Exploring the binding sites and proton diffusion on insulin amyloid fibril surfaces by naphthol-based photoacid fluorescence and molecular simulations

Amdursky, N, Rashid, M, Stevens, M and Yarovsky, I 2017, 'Exploring the binding sites and proton diffusion on insulin amyloid fibril surfaces by naphthol-based photoacid fluorescence and molecular simulations', Scientific Reports, vol. 7, 6245, pp. 1-12.


Document type: Journal Article
Collection: Journal Articles

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Title Exploring the binding sites and proton diffusion on insulin amyloid fibril surfaces by naphthol-based photoacid fluorescence and molecular simulations
Author(s) Amdursky, N
Rashid, M
Stevens, M
Yarovsky, I
Year 2017
Journal name Scientific Reports
Volume number 7
Article Number 6245
Start page 1
End page 12
Total pages 12
Publisher Nature Publishing Group
Abstract The diffusion of protons along biological surfaces and the interaction of biological structures with water are fundamental areas of interest in biology and chemistry. Here, we examine the surface of insulin amyloid fibrils and follow the binding of small molecules (photoacids) that differ according to the number and location of their sulfonic groups. We use transient fluorescence combined with a spherically-symmetric diffusion theory to show that the binding mode of different photoacids determines the efficiency of proton dissociation from the photoacid and the dimensionality of the proton's diffusion. We use molecular dynamics simulations to examine the binding mode and mechanism of the photoacids and its influence on the unique kinetic rates and diffusion properties of the photoacid's dissociated proton, where we also suggest a proton transfer process between one of the photoacids to proximal histidine residues. We show that the photoacids can be used as fluorescent markers for following the progression of amyloidogenic processes. The detailed characterisation of different binding modes to the surface of amyloid fibrils paves the way for better understanding of the binding mechanism of small molecules to amyloid fibrils.
Subject Structural Chemistry and Spectroscopy
Theoretical and Computational Chemistry not elsewhere classified
Biomaterials
DOI - identifier 10.1038/s41598-017-06030-4
Copyright notice This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
ISSN 2045-2322
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