Non-selective ion channel activity of polymorphic human islet amyloid polypeptide (amylin) double channels

Physical Chemistry Chemical Physics : PCCP
Jun ZhaoJie Zheng

Abstract

Fundamental understanding of ion channel formation by amyloid peptides, which is strongly linked to cell toxicity, is very critical for (pre)clinical treatment of neurodegenerative diseases. Here, we combine atomistic simulations and experiments to demonstrate a broad range of conformational states of hIAPP double channels in lipid membranes. All individual channels display high selectivity for Cl(-) ions over cations, but the co-existence of polymorphic double channels of different conformations and orientations with different populations determines the non-ionic selectivity nature of the channels, which is different from the typical amyloid-β channels that exhibit Ca(2+) selective ion-permeable characteristics. This work provides a more complete physicochemical mechanism of amyloid-channel-induced toxicity.

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Citations

Mar 4, 2014·Biochimica Et Biophysica Acta·Jianhan Chen, John M Tomich
Sep 17, 2014·Cell Calcium·Marta S Fernández
Nov 21, 2015·Chemical Communications : Chem Comm·Amit S PithadiaAyyalusamy Ramamoorthy
Dec 10, 2015·Journal of Diabetes Research·Zhenyu QianGuanghong Wei
Dec 10, 2015·Journal of Diabetes Research·Amit PithadiaAyyalusamy Ramamoorthy
Jul 15, 2015·Journal of Chemical Information and Modeling·Mingzhen ZhangJie Zheng
Feb 24, 2015·Physical Chemistry Chemical Physics : PCCP·Mingzhen ZhangJie Zheng
Jun 5, 2014·The Journal of Physical Chemistry Letters·Alex Morriss-Andrews, Joan-Emma Shea
Oct 8, 2020·Molecular Aspects of Medicine·Ji NieXiawei Wei
Sep 10, 2021·Journal of Chemical Information and Modeling·Aliasghar SepehriThemis Lazaridis

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