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

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 dis...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2020-10, Vol.92 (20), p.13822-13828
Main Authors: Townsend, David J, Middleton, David A, Ashton, Lorna
Format: Article
Language:English
Subjects:
Amyloid - chemistry
Amyloidosis
Analytical chemistry
Anticoagulants
Apolipoprotein A
Apolipoprotein A-I
Apolipoprotein A-I - chemistry
Apolipoprotein A-I - genetics
Apolipoprotein A-I - metabolism
Arteriosclerosis
Atherosclerosis
Chemistry
Correlation analysis
Fibrils
Glycosaminoglycans
Heparan sulfate
Heparin
Heparin - chemistry
Heparin - metabolism
Humans
Perturbation
Protein Aggregates
Protein Binding
Protein interaction
Protein structure
Protein Structure, Secondary
Proteins
Raman spectroscopy
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Secondary structure
Spectroscopy
Spectrum analysis
Spectrum Analysis, Raman - methods
Two dimensional analysis
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Summary: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.
ISSN:0003-2700
1520-6882
DOI:10.1021/acs.analchem.0c02390