Gruppenbild AG Huster
Workgroup Daniel Huster

CV Daniel Huster

  • 1/20 – 7/20: Sabbatical at the Department of Chemistry, Tata Institute of Fundamental Research, Mumbai, India
  • 1/14 – 7/14: Sabbatical at the Department of Chemistry, Tata Institute of Fundamental Research, Mumbai, India
  • since 10/08: Head of the Institute for Medical Physics and Biophysics, Leipzig University, Germany (Full professorship for Medical Biophysics)
  • 1/06-9/08: Head of Junior Research Group „Structural Biology of Membrane Proteins“, Institute of Biotechnology, Martin Luther University Halle-Wittenberg, Germany
  • 9/2001-12/2005: Head of Junior Research Group ‚Solid-state NMR studies of membrane-associated proteins‘, Biotechnological-Biomedical Center, Leipzig University, Germany
  • 12/99-8/01: Post doctoral fellow, Department of Chemistry, Iowa State University, Ames, IA, USA
  • 7/99-11/99: Post doctoral fellow, Institute for Medical Physics and Biophysics, Leipzig University, Germany
  • 4/96-6/99: Graduate student, Institute for Medical Physics and Biophysics, Leipzig University, Germany and Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, Rockville, USA. Ph.D. Thesis: „NMR-Untersuchungen zur Wechselwirkung von biologisch relevanten Polyelektrolyten mit Lipidmembranen und Lipoproteinen„, Leipzig University, 1999
  • 9/94-2/96: Diploma thesis, Institute for Medical Physics and Biophysics, Leipzig University, Germany and Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, Bethedsa, USA. Diploma thesis: „NMR-Untersuchungen zur Wasserpermeation von Phospholipidbilayern“ Leipzig University, 1996
  • 10/90-8/94: Undergraduate student, Leipzig University


Institute Director

Porträt Daniel Huster

Prof. Dr. Daniel Huster

Härtelstr. 16-18, 04107 Leipzig
Room 148
Phone +49(0)341 97-15701

Consultation hours:
during the semester: Friday 13:00 – 14:00,
or by email appointment


Astrid Abel
Room 149
Phone +49(0)341 97-15700
Fax     +49(0)341 97-15709

Office hours:
Mo – Thu 8:00 – 14:30


Adler, Juliane, Dr. rer. nat., research associate, Coordinator SFB 1423

Döbel, Viola, technical assistant

Engberg, Oskar, Dr. rer. nat., PostDoc

Fandrei, Ferdinand, doctoral student

Fischer, Markus, doctoral student

Gozzi, Marta, Dr. rer. nat., PostDoc

Keller, Mario, engineer

Korn, Alexander, doctoral student

Laugwitz, Jeannette, doctoral student

Montag, Cindy, technical assistant

Pacull, Emelyne, doctoral student

Penk, Anja, Dr, rer, nat., PostDoc

Scheidt, Holger A., Dr. rer. nat., research associate

Schmidt, Peter, Dr. rer. nat., research associate

Schulze, Christian, PhD student

Schwarze, Benedikt, Dr. rer. nat., PostDoc

Smith-Penzel, Albert A.. PhD, research associate

Voitel, Matthias, doctoral student

Journal Articles

215.  John, T., Adler, J., Elsner, C., Petzold, J., Krueger, M., Martin, L.L., Huster, D., Risselada, H.J., Abel, B. Mechanistic insights into the size-dependent effects of nanoparticles on inhibiting and accelerating amyloid fibril formation. J. Colloid Interface Sci. (2022), in press. [DOI]

214. Musabirova, G., Engberg, O., Gupta, A., Saha Roy, D., Maiti S., Huster, D. Serotonergic drugs modulate the phase behavior of complex lipid bilayers. Biochimie (2022), in press.

213.  Fandrei, F., Engberg, O., Opálka, L., Jancálková, P., Pullmanová, P., Steinhart, M., Koválcik, A., Vávrová, K., Huster, D. Cholesterol sulfate fluidizes the sterol fraction of the stratum corneum lipid phase and increases its permeability. J. Lipid Res. 63 (2022), in press. [PubMed; DOI]

212. Vu, O., Bender, B.J., Pankewitz, L., Huster, D. Beck-Sickinger, A.G., Meiler, J. The structural basis of peptide binding at class A G protein-coupled receptors. Molecules 27 (2022) 210. [DOI]

211. Smith, A.A., Vogel, A., Engbert, O., Hildebrand, Huster, D. A method to construct the dynamic landscape of a bio-membrane with experiment and simulation. Nat. Commun. 13 (2021) 108. [DOI]

210. Dey, S., Surendran, D., Engberg, O., Gupta, A., Fanibunda, S., Das, A., Maity B.K., Dey, A., Visvakarma, V., Kallianpur, M., Scheidt, H.A., Walker, G., Vaidya, V., Huster, D., Maiti, S. Receptor-independent membrane mediated pathways of serotonin action. Chemistry 27 (2021) 7533-7541. [DOI]

209. Fritzsch, J., Korn, A., Surendran, D., Krueger, M., Scheidt, H.A., Maiti, S. Huster, D. Probing the influence of single site mutations in the central cross-β region of amyloid β (1-40) peptides. Biomolecules 11 (2021) 1848. [DOI]

208. Schwarze, B., Korn, A., Höfling, C., Zeitschel, U., Krueger, M., Roßner, S., Huster, D. Peptide backbone modifications of amyloid-β impact fibrillation behavior and neuronal toxicity.  Sci. Rep. 11 (2021) 23767. [DOI]

207. Shurshalova, G.S., Scheidt, H.A., Fischer, M., Huster, D., Aganov, A.V., Klochkov, V.V. Interaction of the pitavastatin with model membranes. Biochem. Biophys. Rep. 28 (2021) 101143. [DOI]

206. Künze, G., Huster, D., Samsonov, S. Investigation of the structure of regulatory proteins interacting with glycosaminoglycans by NMR spectroscopy and molecular modeling – the beginning of a wonderful friendship. Biol. Chem. 402 (2021) 1337-1355. [DOI; PubMed]

205. Pacull, E.M., Sendker, F., Bernhard, F., Scheidt, H.A., Schmidt, P., Huster, D., Krug, U. Integration of cell-free expression and solid-state NMR to investigate the dynamic properties of different sites of the growth hormone secretagogue receptor. Front. Pharmacol. 11 (2020) 562113. [DOI]

204. Vogel, A., Bosse, M., Gauglitz, M., Wistuba, S., Schmidt, P., Kaiser, A., Vsevolod, G., Beck-Sickinger, A.G., Hildebrand, P.W., Huster, D. The dynamics of the neuropeptide Y receptor type 1 investigated by solid-state NMR and molecular dynamics simulation. Molecules 25 (2020) 5489. [DOI; PubMed]

203.  Bochicchio, A, Brandner, A.F., Engberg, O., Huster, D., Böckmann, R. Spontaneous membrane nanodomain formation in the absence and in the presence of the neurotransmitter serotonin. Front. Cell. Dev. Biol.  8 (2020) 601145. [DOI]

202. Krug, U., Gloge, A., Schmidt, P., Becker-Baldus, J., Berhard, F., Kaiser, A., Montag, C. Gauglitz, M., Vishnivetskiy, S.A., Gurevich, V.V., Beck-Sickinger, A.G., Glaubitz, C., Huster, D. The conformational Equilibrium of the neuropeptide Y2 receptor. Angew. Chem. Int. Ed. 59 (2020) 23854-23861. [DOI]

201.  Engberg, O., Bocchicchio, A., Brandner, A.F., Gupta, A., Dey, S., Maiti, S., Böckmann, R.A., Huster, D. Serotonin alters the Phase equilibrium of a ternary mixture of phospholipids and cholesterol. Front. Physiol. 11 (2020) e589969. [DOI]

200. Kremkow, J., Luck, M., Huster, D., Müller, P., Scheidt., H.A. Membrane interaction of ibuprofen with cholesterol-containng lipid membranes. Biomolecules 10 (2020) e1384. [DOI]

199. Scheidt, H.A., Kolocaj, K., Konrad, D., Frank, J.A., Trauner, D., Langosch, D., Huster, D. Light-induced Lipid mixing implies a causal role of Lipid splay in Membrane Fusion. Biochim. Biophys. Acta 1862 (2020) 183438. [DOI]

198. Engberg, O., Kováčik, A., Pullmannová, P., Juhaščik, M., Opálka, L., Huster, D., Vávrová, K. The sphingosine and acyl chains of ceramide [NS] show very different structure and dynamics challenging our understanding of the skin barrier. Angew. Chem. Int. Ed. 59 (2020) 17383-17387. [DOI]

197.  Hutchison, J.M., Shih, K.C., Scheidt, H.A., Fantin, S.M., Parson, K.F., Pantelopulos, G.A., Harrington, H.R., Mittendorf, K.F., Qian, S., Stein, R.A., Collier, S.E., Chambers, M.G., Huang, L., Mittal, R., Katsaras, J., Voehler, M.W., Ruotolo, B.T., Huster, D., McFeeters, R.L., Straub, J.E., Nieh, M.P., Sanders, C.R. Preparation and characterization of bicelles rich in both sphingolipids and cholesterol to study type I and II membrane Proteins. J. Am. Chem. Soc. 142 (2020) 12715-12729. [DOI]

196.  Haralampiev, I., Alonso, D.J., Luck, M., Fischer, M., Abel, T., Huster, D., Di Lella, S., Scheidt, H.A., Müller, P. Interaction of the small-molecule Kinase inhibitors tofacitinib and lapatinib with membranes. Biochim. Biophys. Acta 1862 (2020) 183414. [DOI]

195. Scheidt, H.A., Das, A., Korn, A., Krueger, M., Maiti, S., Huster, D. Structural characteristics of oligomers formed by pyroglutamate-modified amyloid ß peptides studied by solid-state NMR. Phys. Chem. Chem. Phys. 22 (2020) 16887-16895. [DOI]

194. Korn, A., Höfling, C., Zeitschel, U., Krueger, M., Roßner, S., Huster, D. Incorporation of the non-proteinaceous amino Acid β-methyl-amino-alanine affects amyloid β aibril aroperties and aoxicity” ACS Chem. Neurosci. 11 (2020) 1038-104711. [DOI]

193.  Heinrich, F., Salyapongse, A., Kumagai, A., Dupuy, F. G., Shukla, K., Penk, A., Huster, D., Ernst, R. K., Pavlova, A., Gumbart, J. C., Deslouches, B., Di, Y. P., & Tristram-Nagle, S. Synergistic biophysical techniques reveal structural mechanisms of engineered cationic antimicrobial peptides in lipid model membranes. Chemistry 26 (2020) 6247–6256. [DOI]

192.  Förster, Y., Schulze, S., Penk, A., Neuber, C., Möller, S., Hintze, V., Scharnweber, D., Schnabelrauch, M., Pietzsch, J., Huster, D., Rammelt, S. The influence of different artificial extracellular matrix implant coatings on the regeneration of a critical size femur defect in rats,
Mat. Science Engin. 116 (2020) 111157. [DOI]

191.  Nikitina, L.E., Pavelyev, R.S., Startseva, V.A., Kiselev, S.V., Galiullina, L.F., Aganova, O.V., Timerova, A.F., Boichuk, S.V., Azizova, Z.R., Klochkov, V.V., Huster, D., Khodov, I.A., Scheidt, H.A. Structural details on the interaction of biologically active sulfur-containing monoterpenoids with lipid membranes. J. Mol. Liquids 301 (2020) e112366. [DOI]

190. Engberg, O., Scheidt, H.A., Nyholm, T.K.M., Slotte, P., Huster, D. Membrane localization and lipid interactions of common lipid-conjugated fluorescence probes. Langmuir 35 (2019) 1192-11911. [DOI; PubMed]

189. Kumar, S., Scheidt, H.A., Kaur, N., Kang, S., Huster, D., Mithu, V.S. Effect of the alkyl chain length of amphiphilic ionic liquid on the structrue and dynamics of model lipid membranes. Langmuir 35  (2019) 12215-12223. [DOI; PubMed]

188.  Penk, A., Baumann, L, Huster, D., Samsonov, S.A. NMR and molecular modeling reveal the specificity of the interactions between CXCL14 and glycosaminoglycans. Glycobiology 29 (2019) 715-725. [DOI; PubMed]

187.  Bosse, M., Sibold, J., Scheidt, H.A., Patalag, L.J., Kettelhoit, K., Ries, A., Werz, D.B., Steinem, C., Huster, D. Shiga toxin binding alters packing and the domain structure of Gb3-containg membranes: A solid-state NMR study. Phys. Chem. Chem. Phys. 21 (2019) 15630-15638. [DOI; PubMed]

186.  Fränzl, M., Thalheim, T., Adler, J., Huster, D., Posseckardt, J., Mertig, M, Cichos, F. “Thermophoretic trap for single amyloid fibril and protein aggregation studies”. Nat. Methods 16 (2019) 611-614. [DOI; PubMed]

185.  Götz, A., Kamp, F., Mylonas, N., Högel, P., Silber, M., Heinel, H., Menig, S., Vogel, A., Feyrer, H., Huster, D., Luy, B., Langosch, D., Scharnagl, C., Muhle-Goll, C., Steiner, H.  Modulating hinge flexibility in the APP transmembrane domain alters γ-secretase cleavage. Biophys. J. 116 (2019) 2103-2120. [DOI; PubMed]

184.  Galiullina, L.F., Scheidt, H.A., Huster, D., Aganov, A.V., Klochkov, V.V. Interactionof statins with phospholipid bilayers studied by solid-state NMR spectroscopy. Biochim. Biophys. Acta, Biomembr. 1861 (2019) 584-593. [DOI; PubMed]

183.    Bender, B. J., Vortmeier, G., Ernicke, S., Bosse, M., Kaiser, A.,  Els-Heindl, S., Krug, U., Beck-Sickinger, A. G., Meiler, J., Huster, D. Structural model of ghrelin bound to its G protein-coupled receptor. Structure 27 (2019) 537-544.e4. [DOI, PubMed]

182.    Anders, G., Hassiepen, U., Theisgen, S., Heymann, S., Müller, L., Panigada, T., Huster, D., Samsonov, S.A. the intrinsic Pepsin resistance of Interleukin-8 can be explained from a combined bioinformatical and experimental Approach. IEEE/ACM Transactions on Computational Biology and Bioinformactics 15 (2018) 300-308. [DOI]

181.    Kumar, S., Scheidt., H.A., Kaur, N., Kaur, A., Kang, T.S., Huster, D., Mithu, V.S. Amphiphilic ionic liquid-induced membrane permeabilization-binding is not enough. J. Phys. Chem. B. 122 (2018) 6763-6770. [PubMed; DOI]

180.    Scheidt, H.A., Kolocaj, K., Kristensen, J.V., Huster, D., Langosch, D. Transmembrane helix induces membrane fusion through lipid binding and splay. J. Phys. Lett. 9 (2018) 3181-3186. [DOI]

179.    Yang, Z., Han, S., Keller, M., Burkert, K., Bender, B.J., Bosse, M., Kaiser, A., Kögler, L.M., Wifling, D., Bernhardt, G., Plank, N., Littmann, T., Schmidt, P., Yi, C., Li, B., Ye, S., Zhang, R., Xu, B., Larhammar, D., Stevens, R.C., Huster, D., Meiler, J., Zhao, Q., Beck-Sickinger, A.G., Buschauer, A., Wu, B. Structural basis of ligand binding modes of neuropeptide Y Y1 receptor. Nature 556 (2018) 520-524. [PubMed; DOI]

178.    Kamp, F., Scheidt, H.A., Winkler, E., Basset, G., Heinel, H., Hutchison, J.M., LaPointe, L.M., Sanders, C.R., Steiner, H., Huster, D. Bexarotene binds to the amyloid precursor protein transmembrane domain, alters its α-helical conformation, and inhibits γ-secretase non-selectively in liposomes. ACS Cem. Neurosci. 9 (2018) 1702-1713 [DOI]

177.    Korn, A., Surendran, D., Krueger, M., Maiti, S., Huster, D. Ring structure modifications of phenylalanine 19 increase fibrillation kinectics and reduce toxicity of amyloid β (1-40). Chem. Comm. 54 (2018) 5430-5433. [DOI]

176.    Kováčik, A., Vogel, A., Adler, A., Pullmannová, P., Vávrová, K., Huster, D. Probing the role of ceramide hydroxylation in skin barrier lipid models by H2 solid-state NMR spectroscopy and X-ray powder diffraction. Biochim. Biophys. Acta 1860 (2018) 1162-1170. [DOI; PubMed]

175.     Schmidt, P., Bender, B.J., Kaiser, A., Gulati, K., Scheidt, H.A., Hamm, H.E., Meiler, J., Beck-Sickinger, A.G., Huster, D. Improved in vitro folding of the Y2 G protein-coupled receptor into bicelles. Front. Mol. Biosci. 4 (2018) e100. [DOI]

174.     Korn, A., Adler, J., McLennan, S., Krueger, M., Surendran, D., Maiti, S., Huster, D. Amyloid β (1-40) toxicity depends on the molecular contact between phenylalanine 19 and leucine 34. ACS Chem. Neurosci. 9 (2018) 790-799. [DOI, PubMed]

173.     Hoffmann, F., Adler, J., Chandra, B., Mote, K.R., Bekçioğlu-Neff, G., Sebastiani, D., Huster, D. Perturbation of the F19-L34 contact in amyloid β (1-40) fibrils induces only local structural changes but abolishes cytotoxicity. J. Phys. Chem. Lett. 8 (2017) 4740-4745. [PubMed]

172.     Scheidt, H.A., Adler, J., Zeitschel, U., Höfling, C., Korn, A., Krueger, M., Roßner, S, Huster, D. Pyroglutamate-modified amyloid β (11-40) fibrils are more toxic than wildtype fibrils but structurally very similar. Chemistry 23 (2017) 15834-15838. [DOI]

171.     Stahlberg, S., Eichner, A., Sonnenberger, S., Lange, S., Schmitt, T., Demé, B., Hauß, T., Dobner, B., Neubert, R.H.H., Huster, D. The influence of a novel dimeric ceramide molecule on the structure and the thermotropic phase behavior of a stratum corneum model mixture.  Langmuir 33 (2017) 9211-9221. [DOI]

170.     Haralampiev, I., Scheidt, H.A., Huster, D., Müller, P. The potential of α-spinasterol to mimic the membrane properties of natural cholesterol. Molecules 22 (2017) 1390. [DOI]

169.    Hilsch, M., Haralampiev, I. Müller, P., Huster, D., Scheidt, H.A. Membrane properties of hydroxycholesterols related to the brain cholesterol metabolism. Beilstein J. Org. Chem. 13 (2017) 720-727. [DOI]

168.    Schrottke, S., Vortmeier, G., Els-Heindl, S., Bosse, M., Schmidt, P., Scheidt, H.A., Beck-Sickinger, A.G., Huster, D. Expression, functional characterization, and solid-state NMR invextigation of the G protein-coupled GHS receptor in bilayer membranes. Sci. Rep. 7 (2017) 46128. [DOI]

167.    Chandra, B., Halder S., Adler, J., Korn, A., Huster, D., Maiti, S. Emerging structural details of transient amyloid-ß oligomers suggest designs for effective small molecule modulators. Chem. Phys. Lett. 675 (2017) 51-55. [DOI]

166.  Schroeter, A., Stahlberg, S., Školová, B., Sonnenberger, S., Eichner, A., Huster, D., Vávrová, K., Hauß, T., Dobner, B., Neubert, R.H.H., Vogel, A. Phase separation in stratum corneum lipid model membranes based on ceramide [NP]: neutron diffraction and solid-state NMR. Soft Mat. 13 (2017) 2107-2119. [DOI]

165.  Chandra, B., Korn, A., Maity, B.K., Adler, J., Rawat, A., Krueger, M., Huster, D., Maiti, S. Stereoisomers probe steric zippers in amyloid-ß. J. Phys. Chem B. 121 (2017) 1835-1842. [DOI]

164.  Lede, V., Meusel, A., Garten, A., Popkova, Y., Franke, C., Ricken, A., Schulz, A., Kiess, W., Huster, D., Schöneberg, T., Schiller, J. Altered hepatic lipid metabolismn in mice lacking both the melanocortin type 4 receptor and low density lipoprotein receptor. PLoS One 12 (2017) e0172000. [DOI]

163. Eichner, A., Stahlberg, S., Sonnenberger, S., Lange, S., Dobner, B., Ostermann, A., Schrader, T.E., Hauß, T., Schröter, A., Huster, D., Neubert, R.H.H. Influence of the penetration enhancer isopropyl ristate on stratum corneum lipid model membranes revealed by neutron diffraction and 2H NMR experiments. Biochim. Biophys. Acta 1859 (2017) 745-755. [DOI]

162. Adler, J., Scheidt, H.A., Lemmnitzer, K., Krüger, M., Huster, D. N-terminal lipid conjugation leads to the formation of N-terminally extended fibrils. Phys. Chem. Chem. Phys. 19 (2017) 1939-1846. [DOI]

161.  Lede, V., Franke, C., Meusel, A.,  Teupser, D., Ricken, A.,  Thiery, J., Schiller, J., Huster, D., Schöneberg, T., Schulz, A. Severe atherosclerosis and hypercholesterolemia in mice lacking both the melanocortin type 4 receptor and low density lipoprotein receptor. PLoS One 11 (2016) e0167888.

160. Haralampiev, I. , Scheidt, H.A., Abel, T., Luckner, M., Herrmann, A., Huster, D., Müller, P. The interaction of sorafenib and regorafenib with membranes is modulated by their lipid composition. Biochim. Biphys. Acta 1858 (2016) 2871-2881.

159. Scheidt, H.A., Adler, J., Krueger, M., Huster, D. Fibrils of truncated pyroglutamyl-modified Aß peptide exhibit a similar structure as wildtype mature Aß fibrils. Sci. Rep. 6 (2016) 33531.

158. Adler, J., Baumann, M., Voigt, B., Scheidt, H.A., Bhowmik, D., Häupl, T., Abel, B., Madhu, P.K., Balbach, J., Maiti, S., Huster, D. A detailed analysis of the morphology fibrils of selectively mutated amyloid ß (1-40). Chem. Phys. Chem. 17 (2016) 2744-2753.

157. Panitz, N., Theisgen, S., Samsonov, S.A., Gehrke J.P., Baumann, L., Bellmann-Sickert, K., Pisabarro, M.T., Rademann, J., Huster, D., Beck-Sickinger, A.G. The structural investigation of glycosaminoglycan binding to CXCL12 displays distinct interaction sites. Glycobiology 26 (2016) 1209-1221.

156. Funtan, S., Evagrafova Z., Adler, J., Huster, D., Binder, W.H. Amyloid beta aggregation in the presence of stimuli-responsive polymers. Polymers 8 (2016) 178.

155. Kaiser, M., Penk, A., Franke, H., Krügel, U., Nörenberg W., Huster, D., Schaefer, M. Lack of functional P2X7 receptor aggravates brain edema development after middle cerebral artery occlusion. Purineric Signal 12 (2016) 453-463.

154. Scheidt, H.A., Haralampiev, I., Theisgen, S., Schirbel, A., Sbiera, S., Huster, D., Kroiss, M., Müller, P. The adrenal specific toxicant mitotane directly interacts with lipid membranes and alters membrane properties depending on lipid composition. Mol. Cell. Endocrinol.  428 (2016) 68-81.

153. Stahlberg, S., Lange, S., Dobner, B., Huster, D. Probing the role of ceramide headgroup polarity in short-chain model skin barrier lipid mixtures by 2H solid-state NMR spectroscopy. Langmuir 32 (2016) 2023-2031.

152.  Hammer, N., Huster, D., Boldt, A., Hädrich, C., Koch, H., Möbius, R., Schulze-Tanzil, G., Scheidt, H.A. A preliminary technical study on sodium dodecyl sulfate-induced changes of the nano-structural and macro-mechanical proerties in human iliotibial tract specimens. J. Mech. Behav. Biomed. 61 (2016) 164-173.

151. Vogel, A., Scheidt, H.A., Baek, D.J., Bittman, R., Huster, D. Structure and dynamics of the aliphatic cholesterol side chain in membranes as studied by 2H NMR spectroscopy and molecular dynamics simulation. Phys. Chem. Chem. Phys. 18 (2016) 3730-3738.

150. Köhling, S., Künze, G., Lemmnitzer, K., Bermudez, M., Wolber, G., Schiller, J., Huster, D., Rademann, J. Chemoenzymatic synthesis of nanosulfated   tetrahyaluronan with a paramagnetic tag for studying its complex with interleukin-10. Chemistry 22 (2016) 5563-5574.

149. Künze, G., Vogel, A., Köhling, S., Rademann, J., Huster, D. Identification of  the glycosaminoglycan binding site of interleukin-10 by NMR spectroscopy. J. Biol. Chem. 291 (2016) 3100-3113.

148. Nowald, C., Penk, A., Chiu, H., Bein, T., Huster, D., Lieleg, O. A selective mucin/methylcellulose hybrid gel with tailored mechanical properties. Macromol. Biosci. 16 (2016) 567-579.

147. Losensky, L., Goldenbogen, B., Holland, G., Laue, M., Petran, A., Liebscher, J., Scheidt, H.A., Vogel, A., Huster, D., Klipp, E., Arbzuova, A. Micro- and nano-tubules built from loosely and tightly rolled up sheets. Phys. Chem. Chem. Phys. 18 (2016) 1292-1301.

146.  Iseli, H.P., Körber, N., Koch, C., Karl, A., Penk, A., Huster, D., Reichenbach, A., Wiedemann, P., Francke, M. Scleral cross-linking by riboflavin and blue light application in young rabbits: damage threshold and eye growth inhibition. Graefes Arch. Clin. Exp. Ophthalmol. 254 (2016) 109-122.

145. Denz, M., Haralampiev, I., Schiller, S., Szente, L., Herrmann, A., Huster, D., Müller, P. Interaction of fluorescent phospholipids with cyclodextrins.  Chem. Phys. Lipids 194 (2016) 37-48.

144. Hofmann, T., Samsonov, S.A., Pichert, A., Lemmnitzer, Kl, Schiller, J., Huster, D., Pisabarro, M.T., von Bergen, M., Kalkhof, S. Structure analysis of the interleukin-8/glycosaminoglycan interactions by amide hydrogen/deuterium exchange mass spectrometry. Methods 89 (2015) 45-53.

143. Robalo, J.R., Ramalho, J.P.P., Huster, D., Loura, L.M.S.Influence of the sterol aliphatic side chain on membrane properties: a molecular dynamics study.Phys. Chem. Chem. Phys.17 (2015) 22736-22748.  

142. Iseli, H.P., Körber, N., Koch, C., Karl, A., Penk, A., Schuldt, C., Liu, Q, Huster, D., Käs, J.A., Reichenbach, A., Wiedemann, P., Francke, M. Damage threshold in adult rabbit eyes after scleral crosslinking by riboflavin/blue light application. Exp. Eye Res. 139 (2015) 37-47.

141. Scheidt, H.A., Klingler, J., Huster, D., Keller, S. Structural Thermodynamics of myr-Scr(2-19) binding to phospholipid membranes. Biophys. J. 109 (2015) 586-594.

140. Das, A.K., Rawat, A., Bhowmik, D., Pandit, R., Huster, D., Maiti, S. An early folding contact between Phe19 and Leu34 is critical for amyloid-ß oligomer toxicity. ACS Chem. Neurosci. 6 (2015), 1290-1295.

139. Stahlberg, S., Školová. B., Madhu, P.K., Vogel, A., Vávrová, K., Huster, D. Probing the role of ceramide acyl chain length and sphingosine unsaturation in model skin barrier lipid mixtures by 2H solid-state NMR spectroscopy. Langmuir 31 (2015) 4906-4915.

138. Vortmeier, G., DeLuca, S.H., Cholet, C., Scheidt, H.A., Beck-Sickinger, A.G., Meiler, J., Huster, D. Integrating solid state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin. PLoS One (2015) e0122444.

137. Kaiser, A., Müller, P., Zellmann, T., Scheidt, H.A., Bosse, M., Meier, R., Meiler, J., Huster, D., Beck-Sickinger, A., Schmidt, P. Unwinding of the C-terminal residues of the of neuropeptide Y is critical for the Y2 receptor binding and activation. Angewandte Chemie Int. Ed. 54 (2015) 7446-7449.

136. Gopalswamy, M., Kumar, A., Adler, J., Baumann, M., Kumar, S.T., Fändrich, M., Scheidt, H.A., Huster, D., Balbach, J. Structural characterization of amyloid fibrils from the human parathyroid hormone. Biochim. Biophys. Acta (Proteins and Proteomics) 1854 (2015) 249-257.

135.Thomas, L., Kahr, J., Schmidt, P., Krug, U., Scheidt, H.A., Huster, D. The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy. NMN 61 (2015) 347-359.


134. Meyer, T., Baek D.J., Bittman, R., Haralampiev, I., Müller, P., Herrmann, A., Huster, D., Scheidt, H.A. Membrane properties of choloesterol analogs with an unbranched aliphatic side chain. Chem. Phys. Lipids 184 (2014) 1-6.

133. Hammer, N., Huster, D., Fritsch, S., Hädrich, C., Koch, H., Schmidt, P., Sichting, F., Wagner, M., Boldt, A. Do cells contribute to tendon and ligament biomechanics? PLOS One 9 (2014) e105037.

132. Margetić, A., Nannemann, D., Meiler, J., Huster, D., Theisgen, S. Guanylate cyclase-activating protein-2 undergoes structural changes upon binding to lipid surfaces. Biochim. Biophys. Acta 1838 (2014) 2767-2777.

131. Künze G., Gehrcke, J.P., Pisabarro, M.T., Huster, D.  NMR characterization of the binding properties and conformation of glycosaminoglycans interacting with interleukin-10”. Glycobilogy 24 (2014) 1036-1040.

130. Huster, D., Madhu, P.K. Simplifying solid-state NMR spectra for biophysical studies on membrane proteins: Selective targeting of  sites and interactions. Biophys. J. 106 (2014) 2083-2084.

129. Vogel, A., Scheidt, H.A., Feller, S.E., Metso, J., Badeau, R.M., Tikkanen, M.J., Wähälä, K., Jauhiainen, M., Huster, D. The orientation and dynamics of estradiol and estradiol oleate in lipid membranes and HDL disc models. Biophys. J. 107 (2014) 114-125.

128. van Amerongen, Y.F., Roy, U., Spaink, H.P., de Groot, H.J.M., Huster, D., Schiller, J., Matysik, A. Zebrafish brain lipid characterization and quantification by 1H nuclear magnetic resonance spectroscopy and MALDI-TOF mass spectrometry. Zebrafish 11 (2014) 240-247.

127. Schade, M., Berti, D., Huster, D., Herrmann, A., Arbuzova, A. Lipophilic nucleic acids – organization and functionalization of surfaces. Adv. Colloid Interface Sci. 208 (2014) 235-251.

126. Raz, Y., Adler, J., Vogel, A. Scheidt, H.A., Häupl, T., Abel, B., Huster, D., Miller, Y. The influence of  the  ΔK280 mutation and N- or C-terminal extensions on the structure and dynamics of the Tau R2 repeat. Phys. Chem. Chem. Phys. 16 (2014) 7710-7717.

125. Schmidt, P., Scheidt, H., Thomas, L., Müller, P., Huster, D. The G protein-coupled neuropeptide Y receptor type 2 is highly dynamic in lipid membranes as revealed by solid-state NMR spectroscopy. Chem. Eur. J. 20 (2014) 4986-4992.

123. Sansonov, S.A., Theisgen, S., Riemer, T., Huster, D., Pisabarro, M.T. Quantum mechanical, molecular dynamics and NMR studies of glycosaminoglycan monosaccharide blocks. BioMed Res. Int. 2014: 808071 .

124. Vogel, A., Nikolaus, J., Weise, K, Triola, G., Waldmann, H., Winter, R., Herrmann, A., Huster, D. Interaction of the human n-ras protein with lipid raft model membranes of varying degrees of complexity. Biol. Chem. 395 (2014) 779-789.

122. Huster, D. Solid state NMR spectroscopy to study protein-lipid interactions. BBA Molecular and Cell Biology of Lipids 1841 (2014) 1146-1160

121. Künze, G., Theisgen, S., Huster, D. Assignment of HN, N, C´, Cα and Cß NMR chemical shifts for murine interleukin-10. Biomol. NMR Assign. 8 (2014) 375-378. 

120. Adler, J., Scheidt, H.A., Krüger, M., Thomas, L., Huster, D. Local interactions influence the fibrillation kinetics, structure and dynamics of Aß(1-40) but leave the general fibril structure unchanged. Phys. chem. Chem. Phys. 16 (2014) 7461-7471. 

119. Schulz, R., Haberhauer, M., Zernia, G., Pösel, C., Somerson, J.S., Huster, D. Comprehensive characterization of chondrocyte cultures in plasma and whole blood biomatrices. J. Tissue. Eng. Regen. Med. 8 (2014) 566-577.

118. Scheidt, H.A., Meyer, T., Nikolaus, J., Baek D.J., Haralampiev, I., Thomas, L., Bittman, R., Müller, P., Herrmann, A., Huster, D. “Cholesterol’s aliphatic side chain structure modulates membrane properties”. Angew. Chemie Int. Ed. 52 (2013) 12848-12851.

117. Möbius, K., Nordsieck, K., Pichert, A., Samsonov, A., Thomas, L., Schiller, J., Kalkhof, S., Pisabarro,  M.T., Beck-Sickinger A.G., Huster, D. Investigation of lysine side chain interactions of interleukin-8 with glycosaminoglycans studied by a methylation-NMR approach. Glycobiology 23 (2013) 1260-1269. 

116. Witte, K., Kaiser, A., Schmidt, P., Splith, V., Thomas, L., Berndt, S., Huster, D., Beck-Sickinger, A.G. Oxidative in vitro folding of a cysteine deficient mutant of the G protein-coupled neuropeptide Y receptor type 2 improves stability at high concentration. Biol. Chem. 394 (2013 1045-1056.

115. Milles, S., Meyer, T., Scheidt, H. A., Thomas, L., Marek, M., Szente, L., Bittman, R., Herrmann, A., Günther-Pomorski, T., Huster, D., Müller, P. Organization of fluorescent cholesterol analogues in lipid bilayers – lessons from cyclodextrin extraction. Biochim. Biophys., Acta 1828 (2013) 1822-1828. 

114. Berger, C., Berndt, S., Pichert, A., Theisgen, S.,  Huster, D. Efficient isotopic tryptophan labeling of membrane proteins by an indole controlled process conduct. Biotechnol. Bioeng. 110 (2013) 1681-1690.

113. Grimm, C., Meyer, T., Czapla, S., Nikolaus, J., Scheidt, H.A., Vogel, A., Herrmann, A., Wessig, P., Huster, D., Müller, P. Structure and dynamics of molecular rods in membranes: Application of a spin-labeld rod. Chem. Eur. J. 19 (2013) 2703-2710.

112. Büttner, M., Möller, S., Keller, M., Huster, D., Schiller, J., Schnabelrauch, M., Dieter, P., Hempel, U. Over-sulfated chonroitin sulfalte derivatives induce osteogenic differentiation of human stromal mesenchymal cells independent of bone morphogenetic protein2 and transforming growth factor-ß signalling. J. Cell. Physiol. 228 (2013), 330-340.

111. Penk, A., Förster, Y., Scheidt, H.A., Nimptsch, A., Hacker, M.C.,  Schulz-Siegmund, M., Ahnert, P., Schiller, J., Rammelt, S., Huster, D. The pore size of PLGA bone implants determines the de novo formation of bone tissue in tibial head defects in rats. Magn. Resonan. Med. 70 (2013) 925-935. 

110. Weise, K., Huster, D.,  Kapoor, S., Triola, G.,  Waldmann, H., Winter, R. Gibbs energy determinants of Lipoprotein insertion into lipid membranes: The case study of ras proteins. Faraday Discuss. 161 (2013) 549-561.

109. Schade, M., Knoll, A., Vogel, A., Seitz, O., Liebscher, J., Huster, D., Herrmann, A., Arbzuova, A. Remote control of lipophiliic nucleic acids domain partitioning by DNA hybridization and enzymatic cleavage. J. Am. Chem. Soc. 134 (2012), 20490-20497.

108. Nordsieck, K., Pichert, A., Samsonov, S.A., Thomas, L., Berger,  C., Pisabarro, M.T., Huster, D., Beck-Sickinger, A.G. Residue 75 of interleukin-8 is crucial for its  interactions with glycosaminoglycans. ChemBioChem 17 (2012) 2558-2566.

107. Weizenmann, N.,  Huster, D., Scheidt, H.A. Interaction of local anaesthetics with lipid bilayers investigated by (1)H MAS NMR spectroscopy.
Biochim. Biophys. Acta 1818 (2012), 3010-3018.

106. Schiller, J., Huster, D. New methods to study the composition and structure of the extracellular matrix in natural and bioengineered tissues. Biomatter 2 (2012) 1-71

105. Scheidt, H.A., Morgado, I, Huster, D. Solid-state NMR supports the model of intramolecular hydrogen bonds in Aβ protofibrils.
J. Biol. Chem. 287 (2012) 22822-22826.

104. Schlorke, D., Thomas, L., Samsonov, S., Huster, D., Arnhold, J., Pichert, A. The influence of glycosaminoglycans on IL-8-mediated functions of neutrophils. Carbohydrate Research 356 (2012) 196-203.

103.  Scheidt, H.A., Morgado, I., Rothemund, S., Huster, D. Dynamics of amyloid ß fibrils revealed by solid-state NMR.  J. Biol. Chem. 287 (2012) 2017-2021.

102.   Böhme, J., Anderegg, U., Nimptsch, A., Nimptsch, K.,  Hacker, M., Schulz-Siegmund, M., Huster, D., Schiller, J. De novo biosynthesis of GAG in the extracellular matrix of skin studies by MALDI MS. Anal. Biochem. 421 (2012) 791-793.

101. Engelbrecht, T.N., Schroeter, A., Hauß, T., Demé, B., Scheid, H.A., Huster, D., Neubert, R.H.H. The impact of ceramide NP and AP  on the nanostructure of stratum corneum lipid bilayer. Part I: Neutron diffraction and 2H NMR studies on multilamellar models based on ceramides with symmetric alkyl chain length distribution. Soft Matter 8 (2012) 2599-2607.

100. Künze, G., Barré, P., Scheidt, H.A., Thomas, L, Eliezer, D., Huster, D. Binding of the three-repeat domain of tau to phospholipid membranes induces an aggregated-like state of the protein. Biochim. Biophys. Acta 1818 (2012) 2302-2313.

99. Pichert, A., Samsonov, S., Theisgen, S., Baumann, L., Schiller, J., Beck-Sickinger, A.G., Huster, D., Pisaborro, M.T. Characterization of the interaction of interleukin-8 with glycosaminoglycans by solution NMR spectroscopy and molecular modelling. Glycobiol. 22 (2012) 134-145.

98.  Bosse, M., Thomas, L., Hassert, R., Beck-Sickinger, A.G., Huster, D., Schmidt, P. Assessment of a fully active class A G protein-coupled receptor isolated from in vitro folding. Biochemistry 50 (2011) 9817-9825.

97. Andjelković, U., Theisgen, S., Scheidt, H.A., Petković, M., Huster, D., Vujčić, Z.  The thermal stability of the external invertase isoforms from saccharomyces cerevisiae correlates with the surface charge density. Biochimie 94 (2011) 510-515.

96. Engel, K.M.Y., Schröck, K., Teupser, D., Holdt, L.M., Tönjes, A., Kern, M., Dietrich, K., Kovacs, P., Krügel, U., Scheidt, H., Schiller, J., Huster, D., Brockmann, G.A., Augustin, M., Thiery, J., Blüher, M., Stumvoll, M., Schöneberg, T., Schulz, A. Reduced food intake and body weight in mice deficient for the G protein-coupled receptor GPR82. PLOS One 6 (2011) e29400.

95. Scheidt, H., Sickert, A., Meier, T., Castellucci, N., Tomasini, C., Huster, D. The interaction of lipid modified pseudopeptides with lipid membranes. Org. Biomol. Chem. 9 (2011) 6998-7006.

94. Theisgen, S., Thomas, L., Schröder, T., Lange, C., Kovermann, M., Balbach, J., Huster, D. The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2. Eur. Biophys. J. 40 (2011) 565-576.

93. Scheidt, H.A., Morgado, I., Rothemund, S., Huster, D., Fähndrich, M.  Solid-state NMR of Aβ protofibrils implies a β-sheet remodelling upon maturation into terminal amyloid fibrils. Angew. Chemie Int. Ed. 50 (2011) 2837-2840.

92. Penk, A., Müller, M., Scheidt, H.A., Langosch, D., Huster, D. Structure and dynamics of the lipid modifications of a transmembrane α-helical peptide determined by 2H solid-state NMR spectroscopy. Biochim. Biophys. Acta 1808 (2011) 784-791.

91. Nimptsch, A., Schibur, S., Ihling, C., Sinz, C., Riemer, T., Huster, D., Schiller, J. Quantitative analysis of denatured collagen by collagenase digestion and subsequent MALDI-TOF mass spectrometry. Cell Tissue Res. 343 (2011) 605-617.

90. Weber,  F., Böhme,  J., Scheidt, H.A., Gründer, W., Rammelt,  S., Schulz-Siegemund, M., Huster, D. 31P and 13C Solid-state NMR spectroscopy to study collagen synthesis and biomineralization in polymer-based bone implants. NMR Biomed. 25 (2011) 464-475.

89. Berger, C., Montag, C., Berndt, S., Huster, D. Optimization of escherichia coli cultivation methods for high yield neuropeptide Y receptor type 2 production. Protein Expr. Purif. 76 (2011) 25-35.

88. Montanha, E.A., Caseli,  L., Kaczmarek,  O., Liebscher, J., Huster, D., Oliveira Jr., O.N. Comparative study of liponucleosides in Langmuir monolayers as cell membrane models. Biophys. Chem. 153 (2011) 154-158.

87. De Azevedo, E.R., Ayrosa, A.M.I.B., Faria, G.C., Rodríguez, H.J.C., Huster, D.,  Bonagamba, T.J. , Pitombo, R.N.M., Rabbani, S.R. The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR. Magn. Reson. Chem. 48 (2010) 704-711.

86. Al-Robaiy, S., Dihazi, H., Kacza, J., Seeger, J., Schiller, J., Huster, D., Knauer, J., Straubinger:, R.K. Metamorphosis of borrelia burgdorferi organisms – RNA, lipid and protein composition in context with the spirochetes‘ shape. J. Basic Microb.50 (2010) 55-517.

85. Loew, M., Springer, R., Scolari, S., Seitz, O., Liebscher, J., Huster, D., Herrmann, A., Arbuzova., A. lipid domain specific recruitment of lipophilic nucleic acids — a key for switchable functionalization of membranes. J. Am. Chem. Soc. 132 (2010) 16066-16072.

84. Pescador, P., Brodersen, N., Scheidt, H.A., Loew, M., Liebscher, J., Herrmann, A., Huster, D., Arbzuova., A. Microtubes self-assembled from a cholesterol-based nucleoside. Chem. Commun. 46 (2010) 5358-5360.

83. Schmidt P., Berger, C., Scheidt, H.A., Berndt, S., Bunge, A., Beck-Sickinger, A.G., Huster, D. A reconstitution protocol for the in vitro folded human G protein-coupled Y2 receptor into lipid environment. Biophys. Chem. 150 (2010) 29-36.

82. Scheidt, H.A., Badeau, R.M., Huster, D. Investigating the membrane orientation and transversal distribution of 17β-estradiol in lipid membranes by solid-state NMR. Chem. Phys. Lipids 163 (2010) 356-361.

81. Schimmer, S., Lindner, D., Schmidt, P., Montag, C., Beck-Sickinger, A.G., Huster, D., Rudolph, R. Functional characterization of the in vitro folded human Y(1) receptor in lipid environment. Protein Peptide Lett. 17 (2010) 605-609.

80. Scheidt, H.A., Magalhães, A., Schibur, S., de Azevedo, E.R., Bonagambo, T.J., Pascui, O., Schulz, R., Reichert, D., Huster, D. The mobility of chondroitin sulfate in articular and artificial cartilage measured by magic-angle spinning NMR spectroscopy. Biopolymers 93 (2010) 520-532.

79. Kaczmarek, O., Scheidt, H.A., Bunge, A., Föse, D., Herrmann, A., Huster, D., Liebscher, J. 2′-Linking of lipids and other functions to nucleosides via 1,2,3-triazoles. Eur. J. Org. Chem. 8 (2010) 1579-1586.

78. Montanha, E.A., Pavinatto, F.J., Caseli, L., Kaczmarek, O., Liebscher, J., Huster, D., Oliveira Jr., O.N. Properties of lipophilic nucleoside monolayers at the air-water interface. Colloid Surface B Biointerfaces 77 (2010) 161-165.

77. Angelici, G., Castellucci, N., Falini, G., Huster, D., Monari, M., Tomasini, C. Pseudopeptides designed to form supramolecular helices: the role of the stereogenic centers. Cryst. Growth Des. 10 (2010) 923–929.

76. Vogel, A., Reuther, G., Roark, M.B., Tan, K.-T., Waldmann, H., Feller, S.E., Huster, D.  Backbone conformational flexibility of the lipid modified membrane anchor of the human n-ras protein investigated by solid-state NMR and molecular dynamics simulation. Biochim. Biophys. Acta 1798 (2010) 275-285.

75. Theisgen, S., Scheidt, H.A., Magalhães, A., Bonagamba, T.J., Huster, D. A Solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate–cyclase activating protein–2. Biochim. Biophys. Acta – Biomembranes 1798 (2010) 266–274.

74. Bunge, A., Loew, M., Pescador, P., Arbuzova, A., Brodersen, N., Kang, J., Dähne, L., Liebscher, J., Herrmann, A., Stengel, G., Huster, D. Functionalization of lipid membranes with lipophilic oligonucleotides on layer-by-layer coated particles. J. Phys. Chem. B 113 (2009) 16425-16434.

73. Schmidt P., Lindner, D., Montag, C., Berndt, S., Beck-Sickinger, A.G., Rudolph, R., Huster, D. Prokaryotic expression, in vitro folding, and molecular pharmacological characterization of the neuropeptide Y receptor type 2. Biotechnol. Progr. 25 (2009) 1732-1739.

72. Vogel, A., Reuther, G., Weise, K., Triola, G., Nikolaus, J., Tan, K.-T., Nowak, C., Herrmann, A., Waldmann, H., Winter, R., Huster, D. Lipid modifications of Ras sense the membrane environment and induce local enrichment. Angew. Chem. Int. Ed. 48 (2009) 8784-8787.

71. Bunge, A., Fischlechner, M., Loew, M., Arbuzova., A., Herrmann, A., Huster, D. Characterization of lipid bilayers adsorbed on spherical LbL-support.
Soft Matter. 5 (2009) 3331-3339.

70. Angelici, G., Falini, G., Hofmann, H.-J., Huster, D., Monari, M., Tomasini, C. Nanofibers from oxazolidi-2-one containing hybrid foldamers: what is the right molecular size? Chem. Eur. J. 15 (2009) 8037-8048.

69. Thomas, L.,  Scheidt, H.A., Bettio, A., Beck-Sickinger, A.G., Huster, D., Zschörnig, O. Membrane interaction of NPY in the presence of negatively charged and zwitterionic phospholipids. Eur. Biophys. J. 38 (2009) 663-677.

68. Scheidt, H.A., Huster, D. Structure and dynamics of the myristoyl lipid modification of a Src peptide determined by 2H solid-state NMR spectroscopy. Biophys. J. 96 (2009) 3663-3672.

67. Nimptsch, A., Schibur, S., Schnabelrauch, M., Fuchs, B., Huster, D., Schiller, J. Characterization of the quantitative relationship between signal-to-noise (S/N) ratio and sample amount on-target by MALDI-TOF MS: Determination of chondroitin sulfate subsequent to enzymatic digestion. Anal. Chim. Acta 635 (2009) 175-182.

66. Hagenau, A., Scheidt, Rammensee, S.,  H.A., Serpell, L., Huster, D., Scheibel, T. Structural analysis of proteinaceous components in byssal threads of the mussel mytilus galloprovincialis. Macromol. Biosci. 9 (2009) 162-168.

65. Loew, M., Kang, Jing, Dähne, L., Hendus-Altenburger, R., Kaczmarek, O., Liebscher, J., Huster, D., Ludwig, K., Böttcher, C., Herrmann, A., Arbuzova, A. Controlled assembly of vesicle-based nanocontainers on Layer-by-Layer particles via DNA hybridisation. Small 5 (2009) 320-323.

64. Bunge, A., Windeck, A.-K., Pomorski, T., Schiller, J., Herrmann, A., Huster, D., Müller, P. Biophysical characterization of a new phospholipid analogue with a spin-labeled unsaturated fatty acid chain. Biophys. J. 96 (2009) 1008-1015.

63. Brunsveld, L., Waldmann, H., Huster, D. Membrane binding of lipidated Ras peptides and proteins – the structural point of view.
Biochim Biophys Acta – Biomembranes. 1788 (2009) 273-288.

62. Angelici, G., Falini, G., Hofmann, H.-J., Huster, D. Monari, M., Tomasini, C. A fiberlike peptide material stabilized by single intermolecular hydrogen bonds. Angew. Chem. Int. Ed. 47 (2008) 8075 – 8078.

61. Sackewitz, M., Scheidt, H.A., Lodderstedt, G., Schierhorn, A., Schwarz, E., Huster, D. Structural and dynamical characterization of fibrils from a disease-associated alanine expansion domain using proteolysis and solid-state NMR spectroscopy. J. Am. Chem. Soc. 130 (2008) 7172–7173.

60. Kaczmarek, O., Brodersen, N., Bunge, A., Löser, L., Huster, D., Herrmann, A., Arbuzova, A., Liebscher, J. Synthesis of nucleosides with 2′-fixed lipid anchors and their behavior in phospholipid membranes. Eur. J. Org. Chem. 11 (2008) 1917–1928.

59. Bunge, A., Müller, P., Stöckl, M., Herrmann, A., Huster, D. Characterization of the ternary mixture of sphingomyelin, POPC, and cholesterol: Support for an inhomogeneous lipid distribution at high temperatures. Biophys. J. 94 (2008) 2680-2690.

58. Vieler, A., Scheidt, H.A., Schmidt, P., Montag, C., Nowoisky, J.F., Lohr, M., Wilhelm, C., Huster, D., Goss, R.  The influence of phase transitions in phosphatidylethanolamine models on the activity of violaxanthin de-epoxidase. Biochim. Biophys. Acta 1778 (2008) 1027-1034.

57. Huster, D. Solid-state NMR studies of collagen structure and dynamics in isolated fibrils and in biological tissues. Ann. Rep. NMR Spectrosc. 64 (2008) 127-159.

56. Scheidt, H.A., Huster, D. The interaction of small molecules with phospholipid membranes studied by 1H NOESY NMR under magic-angle spinning. Acta Pharmacol. Sin. 29 (2008) 35-49.

55. Vogel, A., Schröder, T., Lange, C., Huster, D. Characterization of the myristoyl lipid modification of membrane bound GCAP-2 by 2H solid-state NMR spectroscopy. Biochim.  Biophys. Acta 1768 (2007) 3171-3181  .

54. Brodersen, N., Li, J., Kaczmarek, O., Bunge, A., Löser, L., Huster, D., Herrmann, A., Liebscher, J.  Nucleosides with 5´-fixed lipid groups – synthesis and anchoring in lipid membranes. Eur. J. Org. Chem. 36 (2007) 6060-6069.

53. Vogel, A., Tan, K.-T., Waldmann, H., Feller, S.E., Brown, M.F., Huster, D. Flexibility of Ras lipid modifications studied by 2H solid-state NMR and molecular dynamics simulations. Biophys. J. 93 (2007) 2697-2712.

52. Haberhauer, M., Zernia, G., Schulz, R., Deiwick, A., Schnepp, C., Huster, D., Bader, A. Tissue engineered cartilage constructs grown in allogenous plasma and whole blood nanoscaffolds. Adv. Mater. 20 (2007) 2061-2067.

51. Schiller, J., Müller, M., Fuchs, B., Arnold, K., Huster, D.  31P NMR spectroscopy of phospholipids. From micelles to membranes“. Current Analytical Chemistry 3 (2007) 283-301.

50. Schulz, J., Pretzsch, M., Khalaf, I., Deiwick, A., Scheidt, H.A., von Salis-Soglio, G., Bader, A., Huster; D. Quantitative monitoring of extracellular matrix production in bone implants by 13C and 31P solid-state NMR spectroscopy. Calcif. Tissue Int. 80 (2007) 275-285.

49. Bringezu, F., Majerowitz, M., Wen, S., Reuther, G., Tan, K.-T., Kuhlmann, J., Waldmann, H., Huster, D. Membrane binding of a lipidated N-Ras protein studied in lipid monolayers. Eur. Biophys. J. 36 (2007) 491-498.

48. Scheidt, H.A., Vogel, A., Eckhoff, A., Koenig, B.W., Huster, D.  Solid-state NMR characterization of the putative membrane anchor of TWD1 from arabidopsis thaliana. Eur. Biophys. J. 36 (2007) 393-404.

47. Bunge, A., Kurz, A., Windeck, A.-K., Rost, M., Flasche, W., Liebscher, J., Herrmann, A., Huster, D.  Lipophilic oligonucleotides spontaneously insert into lipid membranes, bind complementary DNA strands, and translocate into lipid disordered domains. Langmuir 23 (2007) 4455-4464.


46. Reuther, G., Tan, K.-T., Vogel, A., Nowak, C., Arnold, K., Kuhlmann, J., Waldmann, H., Huster, D. The  lipidated membrane anchor of full length N-Ras protein shows an extensive dynamics as revealed by solid-state NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 13840-13846.

45. Kurz, A., Bunge, A., Windeck, A.-K., Rost, M., Flasche, W., Arbzuova, A., Strobach, D., Müller, S., Liebscher, J., Huster, D., Herrmann, A.  Lipid-anchored oligonucleotides for stable double helix formation in distinct membrane domains. Angew. Chemie 118 (2006) 4550-4554; Angew. Chemie Int. Ed. 45 (2006) 4440-4444.

44. Reuther, G., Tan, K.-T., Köhler, J., Nowak, C., Pampel, A., Arnold, K., Kuhlmann, J., Waldmann, H., Huster, D. Structural model of the membrane bound C-terminus of lipid-modified human N-Ras protein. Angew. Chemie 118 (2006) 5387-5390; Angew. Chemie Int. Ed. 45 (2006) 5513-5517.

43. Zernia, G., Huster, D. Collagen dynamics in articular cartilage under osmotic pressure. NMR Biomed. 19 (2006) 1010-1019.

42. Schulz, R., Höhle, S., Zernia, G., Zscharnack, M., Schiller, J., Bader, A., Arnold, K., Huster, D. Analysis of extracellular matrix production in artificial cartilage constructs by histology, immunocytochemistry, mass spectrometry, and NMR spectroscopy. J. Nanosci. Nanotech. 6 (2006) 2368-2381.

41. Vagt, T., Zschörnig, O., Huster, D., Koksch, B. Membrane binding and structure of a cationic coiled coil peptide investigated by CD, fluorescence, and solid-state NMR spectroscopy. ChemPhysChem 7 (2006) 1361-1371.

40. Vogel, A., Katzka, C., Waldmann, H., Arnold, K., Brown, M.F., Huster, D. Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR. J. Am. Chem. Soc. 127 (2005) 12263-12272.

39. Scheidt, H.A., Huster, D., Gawrisch, K. Diffusion of cholesterol and its precursors in lipid membranes studied by 1H PFG MAS NMR. Biophys. J. 89 (2005) 2504-2512.

38. Thomas, L., Scheidt, H.A., Bettio, A., Huster, D., Beck-Sickinger, A., Arnold, K., Zschörnig, O. Neuropeptide Y – membrane interaction detected by EPR and NMR spectroscopy. Biochim. Biophys. Acta 1714 (2005) 103-113.

37. Huster, D. Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR. Prog. Nucl. Magn. Reson. Spectrosc. 46 (2005) 79-107.

36. Huster, D., Scheidt, H.A., Arnold, K., Herrmann, A., Müller, P. Desmosterol may replace cholesterol in biological membranes. Biophys. J. 88 (2005) 1838-1844.

35. Scheidt, H.A., Flasche, W., Cismas, C., Rost, M., Herrmann, A., Liebscher, J., Huster, D. Design and application of lipophilic nucleosides as building blocks to obtain highly functional biological surfaces. J. Phys. Chem. B 108 (2004) 16279-16287.

34. Wagner, K., Beck-Sickinger, A.S., Huster, D.  Structural investigations of a human calcitonin-derived carrier peptide in membrane environment by solid-state NMR. Biochemistry 43 (2004) 12459-12468.

33. Huster, D., Naji, L., Schiller, J., Arnold, K.  Dynamics of the biopolymers in articular cartilage studied by magic angle spinning NMR. Appl. Magn. Reson. 27 (2004) 471-487.

32. Scheidt, H.A., Pampel, A., Nissler, L., Gebhardt, R., Huster, D. Investigation of the membrane localization and dynamics of flavonoids by high-resolution magic angle spinning NMR spectroscopy. Biochim. Biophys. Acta 1663 (2004) 97-107.

31. Reichert, D., Pascui, O., deAzevedo, E.R., Bonagamba, T.J., Arnold, K., Huster, D. A solid-state NMR study of the fast and slow dynamics of collagen fibrils at varying hydration. Magn. Reson. Chem. 42 (2004) 276-284.


30. Scheidt, H., Müller, P., Herrmann, A., Huster, D. The potential of fluorescent and spin labeled steroid analogs to mimic natural cholesterol. J. Biol. Chem. 278 (2003) 45563-54569.

29. Barré, P., Zschörnig, O., Arnold, K., Huster, D. Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study. Biochemistry 42 (2003) 8377-8386.

28. Barré, P., Yamaguchi, S., Saito, H., Huster, D.  Backbone dynamics of bacteriorhodopsin as studied by 13C solid-state NMR spectroscopy. Eur. Biophys. J. 32 (2003) 578-584.

27. Huster, D., Vogel, A., Katzka, C., Scheidt, H.A., Binder, H., Zschörnig, O., Dante, S., Gutberlet, T., Waldmann, H., Arnold, K. Membrane insertion of a lipidated ras peptide by FTIR, solid-state NMR, and Neutron diffraction spectroscopy. J. Am. Chem. Soc. 125 (2003) 4070-4079.

26. Vogel, A., Scheidt, H.A., Huster, D. The distribution of lipid attached EPR probes in bilayers. Application to membrane protein topology. Biophys. J. 85 (2003) 1691-1701.

25. Huster, D., Müller, P., Arnold, K., Herrmann, A. The distribution of chain attached 7-nitrobenz-2oxa-1,3-diazol-4-yl (NBD) in acidic membranes determined by 1H MAS NMR spectroscopy. Eur. Biophys. J. 32 (2003) 47-54.

24. Huster, D., Schiller, J., Arnold, K. Comparison of collagen dynamics in cartilage and isolated fibrils by solid-state NMR spectroscopy. Magn. Reson. Med. 48 (2002) 624-632.

23. Hong, M., Yao, X., Jakes, K., Huster, D. Investigation of molecular motions by magic-angle cross-polarization NMR spectroscopy. J. Phys. Chem. B 106 (2002) 7355-7364.

22. Huster, D., Yao, X., Hong, M.  Membrane protein topology probed by 1H spin diffusion from lipids using solid-state NMR spectroscopy. J. Am. Chem. Soc. 124 (2002) 874-883.

21. Huster, D., Yao, X., Jakes, K., Hong, M. Conformational changes of colicin Ia channel-forming Domain upon Membrane binding: a solid-state NMR study. Biochim. Biophys. Acta (Biomembranes) 1561 (2002) 159-170.

20. Yamaguchi, S., Huster, D., Waring, A., Lehrer, R.I., Kearney, W., Tack, B.F., Hong, M. Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy. Biophys. J. 81 (2001) 2203-2214.

19. Huster, D., Xiao, L.,  Hong, M. Solid-state NMR investigation of the dynamics of soluble and membrane-bound colicin Ia channel-forming domain. Biochemistry 40 (2001) 7662-7674.

18. Rödenbeck, M., Müller, M., Huster, D., Arnold, K.  Counterion condensation as saturation effect under the influence of ion hydration.
Biophys. Chem. 90 (2001) 255-268.

17. Huster, D., Müller, P., Arnold, K., Herrmann, A.  Dynamics of membrane penetration of the fluorescent 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD) group attached to an acyl chain of  phosphatidylcholine. Biophys. J. 80 (2001) 822-831.

16. Huster, D., Kuhn, K., Kadereit, D., Waldmann, H., Arnold, K. High resolution magic angle spinning NMR for the investigation of a ras lipopeptide in a lipid membrane. Angew. Chemie 113 (2001) 1083-1085; Angew. Chemie Int. Ed. 40 (2001) 1056-1058.

15. Schiller, J., Naji, L., Huster, D., Kaufmann, J., Arnold, K. 1H and 13C HR-MAS NMR investigations on native and enzymatically-digested cartilage. Evidence for marked differences. in extraction efficiency. MAGMA 13 (2001) 19-27.

14. Huster, D., Yamaguchi, S., Hong, M. Efficient ß sheet structure determination in proteins by solid state NMR spectroscopy. J. Am. Chem. Soc. 122 (2000)  11320-11327.

13. Huster, D., Dietrich, U., Gutberlet, T., Gawrisch, K., Arnold, K.  Lipid matrix properties in cationic membranes interacting with anionic polyelectrolytes – a solid state NMR approach. Langmuir 16 (2000) 9225-9232.

12. Dähnert, K., Huster, D. Thermodynamics of the laminar Donnan system. J. Colloid Interface Sci. 228 (2000) 226-237.

11. Huster, D., Arnold, K., Gawrisch, K. Strength of Ca2+ binding to retinal lipid membranes – consequences for lipid organization.  Biophys. J. 78 (2000) 3011-3018.

10. Naji, L., Kaufmann, J., Huster, D., Schiller, J., Arnold, K. 13C NMR relaxation study on cartilage and cartilage components. The origin of 13C NMR spectra of cartilage. Carbohyd. Res. 327 (2000) 439-446.

9. Feller, S.E., Huster, D., Gawrisch, K. Interpretation of NOESY cross-relaxation rates from MD simulation of a lipid bilayer. J. Am. Chem. Soc. 121 (1999) 8963-8964.

8. Huster, D., Dähnert, K. Comparison of the Poisson-Boltzmann model and the Donnan equilibrium of a polyelectrolyte in salt solution. J. Colloid Interface Sci. 215 (1999) 131-139.

7. Huster, D., Gawrisch, K.  NOESY NMR crosspeaks between lipid headgroups and hydrocarbon chains – spin diffusion or molecular disorder? J. Am. Chem. Soc. 121 (1999) 1992-1993.

6. Huster, D., Paasche, G., Dietrich, U., Zschörnig, O., Gutberlet, T., Gawrisch, K., Arnold, K. Investigation of phospholipid area compression induced by calcium mediated dextran sulfate interaction. Biophys. J. 77 (1999), 879-887.

5. Jin, A.J., Huster, D., Gawrisch, K., Nossal, R. Light scattering characterization of extruded lipid vesicles. Eur. Biophys. J. 28 (1999) 187-199.

4. Huster, D., Arnold, K., Gawrisch, K. Investigation of lipid organization in biological membranes by two-dimensional nuclear Overhauser enhancement spectroscopy. J. Phys. Chem. B 103 (1999) 243-251.

3. Huster, D., Arnold, K. Ca2+-mediated interaction between dextran sulfate and dimyristoyl-sn-glycero-3-phosphocholine surfaces studied by 2H NMR. Biophys. J. 75 (1998) 909-916.

2. Huster, D., Arnold, K., Gawrisch, K. Influence of docosahexaenoic acid and cholesterol on lateral lipid organization in phospholipid membranes.
Biochemistry 37 (1998) 17299-17308.

1. Huster, D., Jin, A.J., Arnold, K., Gawrisch, K.  Water permeability of polyunsaturated membranes measured by 17O NMR. Biophys. J. 73 (1997) 855-864.


Invited Papers/Book Chapters

10. Huster, D. Structural Dynamics of G Protein-Coupled Receptors in Lipid Membranes Investigated by Solid-State-NMR Spectroscopy. In: Separovic, F., Sani, M.-A. (Eds.), Solid-state NMR: Applications in Biomembrane Structure“, The Biophysical Society, IOP Publishing, Bristol (2020), pp. 11-1 – 11-27, ISBN 978-0-7503-2532-5.

09. Huster, D. Solid-State NMR investigations of the hydration and molecular dynamics of collagen in biological tissue. In: Webb, G. (Ed.), „Modern Magnetic Resonance“, 2nd Edition. Springer, Cham  (2018), pp. 363-380, ISBN 978-3-319-28387-6.

08. Vogel, A., Huster, D. Combining NMR Spectroscopy and Molecular Dynamics Simulation and to Investigate the Structure and Dynamics of Membrane Constituents and Membrane-Associated Proteins. In: Chattopadhyay, A. (Ed.), „Membrane Organization and Dynamics“, Springer (2017), pp. 311-350, ISBN: 987-3-319-66600-6.

07. Huster, D. Solid-state NMR Techniques to Study the Molecular Dynamics in Cartilage. In: Xia, Y,, Momot, K. (Eds.), „Biophysics and Biochemistry of Cartilage by NMR and MRI“, RSC Publishing (2017), pp. 279-298, ISBN 978-1-78262-133-1.

06. Zernia, G., Huster, D. Investigation of Tissue Collagen Dynamics by Solid-state NMR Spectroscopy. In: Webb, G. (Ed.) „Handbook of Modern Magnetic Resonance“, Kluwer Academic Publisher (2008), pp. 87-92.

05. Huster, D., Schiller, J., Naji, L., Kaufmann, J., Arnold, K. NMR Studies of Cartilage – Dynamics, Diffusion and Degradation“. In: Haberland, R., Pöppl, A., Stannarius, R., Michel, D. (Eds.), Molecules in Interaction with Surfaces and Interfaces, Lecture Notes in Physics. Springer Verlag, Heidelberg (2004), pp. 465-503.

04. Schiller, J., Huster, D., Fuchs, B., Naji, L., Kaufmann, J., Arnold, K. Evaluation of Cartilage Composition and Degradation by High Resolution Magic Angle Spinning Nuclear Magnetic Resonance. In: De Ceuninck, F., Pastoureau, P., Sabatini, M. (Eds.), „Methods in Molecular Medicine“, Vol. 100, Cartilage and Osteoarthritis, Volume 2, Structure and In Vivo Analysis. Humana Press (2004), pp. 269-287.  

03. Huster, D., Schiller, J., Arnold, K. Dynamics of Collagen in Articular Cartilage Studies by Solid-state NMR Methods. In: De Ceuninck, F., Pastoureau, P., Sabatini, M. (Eds.), „Methods in Molecular Medicine“, Vol. 100, Cartilage and Osteoarthritis, Volume 2, Structure and In Vivo Analysis. Humana Press (2004), pp. 307-322.

02. Schiller, J., Fuchs, B., Huster, D., Naji, L., Arnold, K. Structural Properties of Normal and Diseased Cartilage from the View of Biophysical Chemistry. In: Ramchandran, U. (Ed.) „Recent Research Developments in Biochemistry“, Current Topics in Biochemical Research, Vol. 5, Research Prints, Trivandrum (2003), pp. 43-63.

01. Huster, D., Gawrisch, K. New insights into biomembrane structure from two-dimensional nuclear Overhauser enhancement spectroscopy. In: Katsaqras, J., Gutberlet (Eds.) „Lipid Bilayers Structure and Interactions“. Springer Verlag, Berlin (2000), pp. 109-125


3. Huster, D. Festkörper-NMR-Untersuchungen zur Struktur und Dynamik membrangebundener und Fibrillen bildender Proteine.
Habilitation, University of Leipzig, 2004

2. Huster, D. NMR-Untersuchungen zur Wechselwirkung von biologisch relevanten Polyelektrolyten mit Lipidmembranen und Lipoproteinen.
Ph. D. thesis, University of Leipzig, 1999

1. Huster, D. NMR-Untersuchungen zur Wasserpermeation von Phospholipidbilayern.
Diploma thesis, University of Leipzig, 1996