Resveratrol interferes with the aggregation of membrane-bound human-IAPP: A molecular dynamics study(558 views) Lolicato F, Raudino A, Milardi D, La Rosa C
Keywords: Atomistic Simulation, Membrane, Molecular Dynamics, Resveratrol, Type Ii Diabetes, Amylin, Amyloid, Aqueous Solution, Article, Complex Formation, Drug Protein Binding, Human, Hydrophobicity, Membrane Damage, Molecular Interaction, Protein Aggregation, Protein Secondary Structure,
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Catania, Viale A. Doria 6Catania, Italy
Department of Physics, Tampere University of Technology, P.O. Box 692Tampere, Finland
Istituto di Biostrutture e Bioimmagini, CNR, Unità Organizzativa e di Supporto di Catania, Viale A. Doria 6Catania, Italy
a Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania I-95125, Ita
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Jayasinghe, S. A., Langen, R., Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy (2005) Biochemistry, 44, pp. 12113-12119
Brender, J. R., Salamekh, S., Ramamoorthy, A., Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective (2012) Acc. Chem. Res., 45, pp. 454-462
Sciacca, M. F. M., Pappalardo, M., Milardi, D., Grasso, D. M., La Rosa, C., Calcium-activated membrane interaction of the islet amyloid polypeptide: Implications in the pathogenesis of type II diabetes mellitus (2008) Arc. Biochem. Biophys., 477, pp. 291-298
Goh, K. P., Lee, H. Y., Lau, D. P., Supaat, W., Chan, Y. H., Koh, A. F. Y., Effects of resveratrol in patients with type 2 diabetes mellitus on skeletal muscle SIRT1 expression and energy expenditure (2014) Int. J. Sport Nutr. Exerc. Metab., 24, pp. 2-13
Sciaccaa, M. F. M., Chillemi, R., Sciuto, S., Pappalardo, M., La Rosa, C., Grasso, D., Milardi, D., Interactions of two O-phosphorylresveratrol derivatives with model membranes (2012) Arc. Biochem. Biophys., 521, pp. 111-116
Yonemoto, I. T., Kroon, G. J. A., Dyson, H. J., Balch, W. E., Kelly, J. W., Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state (2008) Biochemistry, 47, pp. 9900-9910
Vaiana, S. M., Best, R. B., Yau, W. M., Eaton, W. A., Hofrichter, J., Evidence for a partially structured state of the amylin monomer (2009) Biophys. J., 97, pp. 2948-2957
Dupuis, N. F., Wu, C., Shea, J. E., Bowers, M. T., The amyloid formation mechanism in human IAPP: Dimers have -strand monomer-monomer interfaces (2011) J. Am. Chem. Soc., 113, pp. 7240-7243
Patil, S. M., Xu, S., Sheftic, S. R., Alexandrescu, A. T., Dynamic alpha-helix structure of micelle-bound human amylin (2009) J. Biol. Chem., 284, pp. 11982-11991
Malde, A. K., Zuo, L., Breeze, M., Stroet, M., Poger, D., Nair, P. C., Oostenbrink, C., Mark, A. E., An automated force field topology builder (ATB) and repository: Version 1. 0 (2011) J. Chem. Theory Comput., 12, pp. 4026-4037
Dewar, M. J. S., Zoebisch, E. G., Healy, E. F., Stewart, J. J. P., The development and use of quantum-mechanical molecular-models 0. 76. AM1-A new general-purpose quantum-mechanical molecular model (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
Zhao, W., R g, T., Gurtovenko, A. A., Vattulainen, I., Karttunen, M., Atomic-scale structure and electrostatics of anionic aalmitoyloleoylphosphatidylglycerol lipid bilayers with Na+ counterions (2007) Biophys. J., 92, pp. 1114-1124
Cino, E. A., Choy, W. -Y., Karttunen, M., Conformational biases of linear motifs (2013) J. Phys. Chem. B, 117, pp. 15943-15957
Gerben, S. R., Lemkul, J. A., Brown, A. M., Bevan, D. R., Comparing atomistic molecular mechanics force fields for a difficult target: A case study on the Alzheimer's amyloid -peptide (2013) J. Biomol. Struct. Dyn., 31, pp. 1-16
Berendsen, H. J. C., Postma, J. P. M., Van Gunsteren, W. F., Hermans, J., Interaction models for water in relation to protein hydration (1981) Intermolecular Forces, pp. 331-342. , B. Pullman (Ed.) D. Reidel, Dordrecht, Holland
Resveratrol interferes with the aggregation of membrane-bound human-IAPP: A molecular dynamics study