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dc.contributor.authorZhang, Ruiyan
dc.contributor.authorZhang, Ning
dc.contributor.authorMohri, Marzieh
dc.contributor.authorWu, Lisha
dc.contributor.authorEckert, Thomas
dc.contributor.authorKrylov, Vadim B.
dc.contributor.authorAntosova, Andrea
dc.contributor.authorPonikova, Slavomira
dc.contributor.authorBednarikova, Zuzana
dc.contributor.authorMarkart, Philipp
dc.contributor.authorGünther, Andreas
dc.contributor.authorNorden, Bengt
dc.contributor.authorBilleter, Martin
dc.contributor.authorSchauer, Roland
dc.contributor.authorScheidig, Axel J.
dc.contributor.authorRatha, Bhisma N.
dc.contributor.authorBhunia, Anirban
dc.contributor.authorHesse, Karsten
dc.contributor.authorEnani, Mushira Abdelaziz
dc.contributor.authorSteinmeyer, Jürgen
dc.contributor.authorPetridis, Athanasios K.
dc.contributor.authorKozar, Tibor
dc.contributor.authorGazova, Zuzana
dc.contributor.authorNifantiev, Nikolay E.
dc.contributor.authorSiebert, Hans-Christian
dc.date.accessioned2021-03-11T10:15:11Z
dc.date.available2021-03-11T10:15:11Z
dc.date.issued2019-02-27
dc.identifier.citationZhang, R., Zhang, N., Mohri, M., Wu, L., Eckert, T., Krylov, V. B., … Siebert, H.-C. (2019). Nanomedical Relevance of the Intermolecular Interaction Dynamics—Examples from Lysozymes and Insulins. ACS Omega, 4(2), 4206–4220. doi:10.1021/acsomega.8b02471
dc.identifier.issn2470-1343
dc.identifier.issn2470-1343
dc.identifier.doi10.1021/acsomega.8b02471
dc.identifier.urihttp://hdl.handle.net/10754/668080
dc.description.abstractInsulin and lysozyme share the common features of being prone to aggregate and having biomedical importance. Encapsulating lysozyme and insulin in micellar nanoparticles probably would prevent aggregation and facilitate oral drug delivery. Despite the vivid structural knowledge of lysozyme and insulin, the environment-dependent oligomerization (dimer, trimer, and multimer) and associated structural dynamics remain elusive. The knowledge of the intra- and intermolecular interaction profiles has cardinal importance for the design of encapsulation protocols. We have employed various biophysical methods such as NMR spectroscopy, X-ray crystallography, Thioflavin T fluorescence, and atomic force microscopy in conjugation with molecular modeling to improve the understanding of interaction dynamics during homo-oligomerization of lysozyme (human and hen egg) and insulin (porcine, human, and glargine). The results obtained depict the atomistic intra- and intermolecular interaction details of the homo-oligomerization and confirm the propensity to form fibrils. Taken together, the data accumulated and knowledge gained will further facilitate nanoparticle design and production with insulin or lysozyme-related protein encapsulation.
dc.description.sponsorshipThis work was supported by the Open Project of Shandong Collaborative Innovation Center for Antibody Drugs (No. CIC-AD1834) and Tai-Shan Scholar Research Fund of Shandong Province of China. This work was also technically supported by Engineering Research Center for Nanomedicine and Drug Delivery Systems. The Swedish NMR Centre is acknowledged for supplying instrument time and support. This work was supported by the King Abdullah University of Science and Technology (grant KUK-11-008-23 awarded to B.N. with Ph.D. position for L.W.) and the European Research Council (ERC-2008-AdG 227700 to B.N.). We thank the Sialic Acids Society for financial support. Parts of the work were supported by RSF grant 14-23-00199 (NEN). On the Slovak side, the work was supported by project VEGA 2/0145/17, 2/0030/18, and SAS-MOST JRP 2015/5. This work was partly supported by Council of Scientific and Industrial Research (CSIR), Govt. of India (02(0292)/17/EMR-II) (to AB). Supports from EU projects 26220120033, 26210120002, 26110230097, and 26210120012 (IEP SAS Kosice, Slovakia) are gratefully acknowledged. We also thank Prof. Dr Frank D Sonnichsen (Otto Diels Institute for Organic Chemistry, Christian Albrechts University, Kiel, Germany) for his helpful support with respect to some of our NMR experiments. Last but not least, Dr Anna Kozarova (University of Windsor, Windsor, Ontario Canada) is highly acknowledged for critical reading and helpful comments on the manuscript.
dc.publisherAmerican Chemical Society (ACS)
dc.relation.urlhttps://pubs.acs.org/doi/10.1021/acsomega.8b02471
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Omega, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acsomega.8b02471.
dc.titleNanomedical Relevance of the Intermolecular Interaction Dynamics—Examples from Lysozymes and Insulins
dc.typeArticle
dc.identifier.journalACS Omega
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionInstitute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, P. R. China
dc.contributor.institutionRI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany
dc.contributor.institutionInstitute of Zoology, Department of Structural Biology, Christian-Albrechts-University, Am Botanischen Garten 1-9, 24118 Kiel, Germany
dc.contributor.institutionDepartment of Chemical and Biological Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
dc.contributor.institutionDepartment of Chemistry and Biology, University of Applied Sciences Fresenius, Limburger Str. 2, 65510 Idstein, Germany
dc.contributor.institutionInstitut für Veterinärphysiolgie und Biochemie, Fachbereich Veterinärmedizin, Justus-Liebig-Universität Gießen, Frankfurter Str. 100, 35392 Gießen, Germany
dc.contributor.institutionLaboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation
dc.contributor.institutionDepartment of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia
dc.contributor.institutionMedical Clinic II, Justus-Liebig-University, Klinikstraße 33, 35392 Giessen, Germany
dc.contributor.institutionPneumology, Heart-Thorax-Center Fulda, Pacelliallee 4, 36043 Fulda, Germany
dc.contributor.institutionDepartment of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden
dc.contributor.institutionInstitute of Biochemistry, Christian-Albrechts-University, Olshausenstrasse 40, 24098 Kiel, Germany
dc.contributor.institutionBiomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India
dc.contributor.institutionTierarztpraxis Dr. Karsten Hesse, Rathausstraße 16, 35460 Stauffenberg, Germany
dc.contributor.institutionInfectious Diseases Division, Department of Medicine, King Fahad Medical City, P.O. Box 59046, 11525 Riyadh, Kingdom of Saudi Arabia
dc.contributor.institutionLaboratory for Experimental Orthopaedics, Department of Orthopaedics, Justus-Liebig-University, Paul-Meimberg-Str. 3, D-35392 Giessen, Germany
dc.contributor.institutionNeurochirurgische Klinik, Universität Düsseldorf, Geb. 11.54, Moorenstraße 5, 40255 Düsseldorf, Germany
dc.contributor.institutionCenter for Interdisciplinary Biosciences, TIP-UPJS, Jesenna 5, 04001 Kosice, Slovakia
dc.identifier.volume4
dc.identifier.issue2
dc.identifier.pages4206-4220
kaust.grant.numberKUK-11-008-23
dc.identifier.eid2-s2.0-85062369515


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