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    Rights statement: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Analytical Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.analchem.0c02390

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    Embargo ends: 16/09/21

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Raman Spectroscopy with 2D Perturbation Correlation Moving Windows for the Characterization of Heparin–Amyloid Interactions

Research output: Contribution to journalJournal articlepeer-review

Published
<mark>Journal publication date</mark>31/10/2020
<mark>Journal</mark>Analytical Chemistry
Issue number20
Volume92
Number of pages7
Pages (from-to)13822–13828
Publication StatusPublished
Early online date16/09/20
<mark>Original language</mark>English

Abstract

It has been shown extensively that glycosaminoglycan (GAG)–protein interactions can induce, accelerate, and impede the clearance of amyloid fibrils associated with systemic and localized amyloidosis. Obtaining molecular details of these interactions is fundamental to our understanding of amyloid disease. Consequently, there is a need for analytical approaches that can identify protein conformational transitions and simultaneously characterize heparin interactions. By combining Raman spectroscopy with two-dimensional (2D) perturbation correlation moving window (2DPCMW) analysis, we have successfully identified changes in protein secondary structure during pH- and heparin-induced fibril formation of apolipoprotein A-I (apoA-I) associated with atherosclerosis. Furthermore, from the 2DPCMW, we have identified peak shifts and intensity variations in Raman peaks arising from different heparan sulfate moieties, indicating that protein–heparin interactions vary at different heparin concentrations. Raman spectroscopy thus reveals new mechanistic insights into the role of GAGs during amyloid fibril formation.

Bibliographic note

This document is the Accepted Manuscript version of a Published Work that appeared in final form in Analytical Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.analchem.0c02390