Conformation change of α-synuclein(61-95) at the air-water interface and quantitative measurement of the tilt angle of the axis of its α-helix by multiple angle incidence resolution spectroscopy

Colloids and Surfaces. B, Biointerfaces
Chengshan WangRoger M Leblanc

Abstract

Various techniques have been developed to determine protein's structure to understand how proteins work.  Compared with X-ray crystallography requiring proteins to form single crystal structure and NMR which usually needs long time measurement, surface FT-IR techniques are able to quickly determine the tilt angle (the key information to determine whether the α-helix is transmembrane) of peptides/proteins in a monolayer at the interface (e.g. membranes). Specifically, for α-helical peptides/proteins in membrane, the tilt angle of the axis is one of the key information. In this paper, Multiple Angle Incidence Resolution Spectroscopy (MAIRS), a recently developed surface FTIR technique, was applied for the first time to quantitatively determine the tilt angle of the axis of α-helical model peptide related to α-synuclein (α-syn). α-Syn is a 140-amino-acid presynaptic protein whose aggregation is the hallmark of Parkinson's disease (PD). It is difficult for α-syn to form a single crystal structure and the primary structure of α-syn constitutes three domains: the N-terminus containing residues 1-60; the nonamyloid component (NAC) which spans residues 61-95 and is highly prone to aggregation; and C-terminus with residues 96-140. Here,...Continue Reading

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Mar 12, 2020·The Journal of Physical Chemistry. a·Nobutaka ShioyaTakeshi Hasegawa

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