Nanomedical Relevance of the Intermolecular Interaction Dynamics-Examples from Lysozymes and Insulins.
Autor: | Zhang R; Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, P. R. China.; RI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany.; Institute of Zoology, Department of Structural Biology, Christian-Albrechts-University, Am Botanischen Garten 1-9, 24118 Kiel, Germany., Zhang N; Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, P. R. China., Mohri M; RI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany., Wu L; Department of Chemical and Biological Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden., Eckert T; Department of Chemistry and Biology, University of Applied Sciences Fresenius, Limburger Str. 2, 65510 Idstein, Germany.; Institut für Veterinärphysiolgie und Biochemie, Fachbereich Veterinärmedizin, Justus-Liebig-Universität Gießen, Frankfurter Str. 100, 35392 Gießen, Germany., Krylov VB; Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation., Antosova A; Department of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia., Ponikova S; Department of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia., Bednarikova Z; Department of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia., Markart P; Medical Clinic II, Justus-Liebig-University, Klinikstraße 33, 35392 Giessen, Germany.; Pneumology, Heart-Thorax-Center Fulda, Pacelliallee 4, 36043 Fulda, Germany., Günther A; Medical Clinic II, Justus-Liebig-University, Klinikstraße 33, 35392 Giessen, Germany., Norden B; Department of Chemical and Biological Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden., Billeter M; Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden., Schauer R; Institute of Biochemistry, Christian-Albrechts-University, Olshausenstrasse 40, 24098 Kiel, Germany., Scheidig AJ; Institute of Zoology, Department of Structural Biology, Christian-Albrechts-University, Am Botanischen Garten 1-9, 24118 Kiel, Germany., Ratha BN; Biomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India., Bhunia A; Biomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India., Hesse K; Tierarztpraxis Dr. Karsten Hesse, Rathausstraße 16, 35460 Stauffenberg, Germany., Enani MA; Infectious Diseases Division, Department of Medicine, King Fahad Medical City, P.O. Box 59046, 11525 Riyadh, Kingdom of Saudi Arabia., Steinmeyer J; Laboratory for Experimental Orthopaedics, Department of Orthopaedics, Justus-Liebig-University, Paul-Meimberg-Str. 3, D-35392 Giessen, Germany., Petridis AK; Neurochirurgische Klinik, Universität Düsseldorf, Geb. 11.54, Moorenstraße 5, 40255 Düsseldorf, Germany., Kozar T; Center for Interdisciplinary Biosciences, TIP-UPJS, Jesenna 5, 04001 Kosice, Slovakia., Gazova Z; Department of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia., Nifantiev NE; Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation., Siebert HC; RI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany. |
---|---|
Jazyk: | angličtina |
Zdroj: | ACS omega [ACS Omega] 2019 Feb 28; Vol. 4 (2), pp. 4206-4220. Date of Electronic Publication: 2019 Feb 27. |
DOI: | 10.1021/acsomega.8b02471 |
Abstrakt: | Insulin 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. Competing Interests: The authors declare no competing financial interest. |
Databáze: | MEDLINE |
Externí odkaz: |