ArticlePloS one2012
Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide.Physical chemistry chemical physics : PCCP · 2017Article
- Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations.Scientific reports · 2017Article
- Conformational Dynamics of the Human Islet Amyloid Polypeptide in a Membrane Environment: Toward the Aggregation Prone Form.Biochemistry · 2016Article
- Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers.Journal of diabetes research · 2016Article
- Free energy simulations of amylin I26P mutation in a lipid bilayer.European biophysics journal : EBJ · 2015Article
- β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH.PloS one · 2014Article
- Membrane permeation induced by aggregates of human islet amyloid polypeptides.Biophysical journal · 2013Article
- Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations.International journal of molecular sciences · 2013Article
- Adsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated Aggregation.International journal of molecular sciences · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
The amyloid fibrils formed by islet amyloid polypeptide (IAPP) are associated with type II diabetes. One of the proposed mechanisms of the toxicity of IAPP is that it causes membrane damage. The fatal mutation of S20G human IAPP was reported to lead to early onset of type II diabetes and high tendency of amyloid formation in vitro. Characterizing the structural features of the S20G mutant in its monomeric state is experimentally difficult because of its unusually fast aggregation rate. Computational work complements experimental studies. We performed a series of molecular dynamics simulations of the monomeric state of human variants in the membrane. Our simulations are validated by extensive comparisons with experimental data. We find that a helical disruption at His18 is common to both human variants. An L-shaped motif of S20G mutant is observed in one of the conformational families. This motif that bends at His18 resembles the overall topology of IAPP fibrils. The conformational preorganization into the fibril-like topology provides a possible explanation for the fast aggregation rate of S20G IAPP.
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Registered trials
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