Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies

Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry
Sandra J MooreRicardo L Mancera

Abstract

Human islet amyloid polypeptide (hIAPP) is a naturally occurring, intrinsically disordered protein whose abnormal aggregation into amyloid fibrils is a pathological feature in type 2 diabetes, and its cross-aggregation with amyloid beta has been linked to an increased risk of Alzheimer's disease. The soluble, oligomeric forms of hIAPP are the most toxic to β-cells in the pancreas. However, the structure of these oligomeric forms is difficult to characterise because of their intrinsic disorder and their tendency to rapidly aggregate into insoluble fibrils. Experimental studies of hIAPP have generally used non-physiological conditions to prevent aggregation, and they have been unable to describe its soluble monomeric and oligomeric structure at physiological conditions. Molecular dynamics (MD) simulations offer an alternative for the detailed characterisation of the monomeric structure of hIAPP and its aggregation in aqueous solution. This paper reviews the knowledge that has been gained by the use of MD simulations, and its relationship to experimental data for both hIAPP and rat IAPP. In particular, the influence of the choice of force field and water models, the choice of initial structure, and the configurational sampling met...Continue Reading

References

Jan 1, 1978·Annual Review of Biochemistry·P Y Chou, G D Fasman
Jul 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·P WestermarkC Betsholtz
Jun 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·P WestermarkK H Johnson
Sep 15, 1988·Biochemical and Biophysical Research Communications·G G GlennerC A Wiley
Dec 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·G J CooperK B Reid
Jun 25, 1996·Proceedings of the National Academy of Sciences of the United States of America·S C LiC M Deber
Jul 9, 1996·Proceedings of the National Academy of Sciences of the United States of America·J JansonP C Butler
Jun 1, 1997·Journal of Structural Biology·C S GoldsburyJ Kistler
May 11, 1999·The American Journal of Pathology·H J Hiddinga, N L Eberhardt
Jul 28, 1999·Protein Science : a Publication of the Protein Society·M K Kim, Y K Kang
Aug 15, 2000·Journal of Structural Biology·C GoldsburyU Aebi
Apr 3, 2003·Experimental Gerontology·Lucy MarzbanC Bruce Verchere
Apr 30, 2003·Biopolymers·Alessandro MascioniGianluigi Veglia
Jan 6, 2004·The Journal of Biological Chemistry·Janelle D GreenUeli Aebi
Jan 20, 2004·Journal of Molecular Biology·O Sumner Makin, Louise C Serpell
Jan 31, 2004·The Journal of Biological Chemistry·Brian O'NuallainRonald Wetzel
Jul 21, 2004·Journal of Computational Chemistry·Chris OostenbrinkWilfred F van Gunsteren
Aug 5, 2004·The Journal of Clinical Endocrinology and Metabolism·Rebecca L HullSteven E Kahn
Aug 24, 2004·Journal of Molecular Biology·Jefferson D Knight, Andrew D Miranker
Sep 11, 2004·The Journal of Biological Chemistry·Sajith A Jayasinghe, Ralf Langen
Sep 7, 2005·Biochemistry·Sajith A Jayasinghe, Ralf Langen
Nov 19, 2005·Proceedings of the National Academy of Sciences of the United States of America·Thorsten LührsRoland Riek
Nov 25, 2006·Protein Science : a Publication of the Protein Society·Jessica A Williamson, Andrew D Miranker
Apr 11, 2007·The Journal of Physical Chemistry. B·Stefano Piana, Alessandro Laio
Jun 17, 2008·Protein Science : a Publication of the Protein Society·Jed J W WiltziusDavid Eisenberg
Nov 19, 2008·Proceedings of the National Academy of Sciences of the United States of America·Anant K ParavastuRobert Tycko
Feb 12, 2009·Physical Biology·Andisheh Abedini, Daniel P Raleigh
Feb 27, 2009·The Journal of Biological Chemistry·Sharadrao M PatilAndrei T Alexandrescu
Apr 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Sang-Hee ShimMartin T Zanni
May 22, 2009·Journal of the American Chemical Society·Ravi Prakash Reddy NangaAyyalusamy Ramamoorthy

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Citations

Mar 17, 2019·International Journal of Molecular Sciences·Anne H S MartinelliRodrigo Ligabue-Braun
Jan 3, 2020·Interdisciplinary Sciences, Computational Life Sciences·Yu WangGuizhao Liang
Jun 10, 2020·Computational and Structural Biotechnology Journal·Wresti L AnggayastiRicardo L Mancera
Dec 1, 2020·International Journal of Biological Macromolecules·Jinming WuHailing Li
Nov 17, 2020·Frontiers in Aging Neuroscience·Gilbert HoMakoto Hashimoto
Apr 23, 2021·Journal of Molecular Graphics & Modelling·Elena A ErmakovaIgor A Sedov
Jun 3, 2021·International Journal of Molecular Sciences·Neret Pujol-NavarroPaul Mulheran
Apr 12, 2019·Chemical Reviews·Ioana M Ilie, Amedeo Caflisch
Aug 29, 2019·Journal of the American Chemical Society·Zachary A LevineJoan-Emma Shea
Sep 29, 2019·The Journal of Physical Chemistry. B·Jean-Marc CrowetLaurence Lins
Aug 10, 2021·Protein and Peptide Letters·Alissa OakesDavid A Moffet

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Methods Mentioned

BETA
electron
atomic force microscopy
X-ray
nuclear
circular dichroism
NMR
electron diffraction
ssNMR
transmission electron microscopy
infrared spectroscopy

Software Mentioned

REST2
REMD
BEMD
HT
AMBER
CHARMM
OPLS
AMBERff99sb
CHARMM22
AMBER99SB

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