Investigation of DMSO-induced conformational transitions in human serum albumin using two-dimensional Raman optical activity spectroscopy

Batista, Andrea N. L. and Batista, Joao M. and Ashton, Lorna and Bolzani, Vanderlan S. and Furlan, Maysa and Blanch, Ewan W. (2014) Investigation of DMSO-induced conformational transitions in human serum albumin using two-dimensional Raman optical activity spectroscopy. Chirality, 26 (9). pp. 497-501. ISSN 0899-0042

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Abstract

Recent Raman and Raman optical activity (ROA) results have demonstrated that dimethyl sulfoxide (DMSO) induces the selective conversion of alpha-helix motifs into the poly(L-proline) II (PPII) helix conformation in an array of proteins, while beta-sheets remain mostly unaffected. Human serum albumin (HSA), a highly alpha-helical protein, underwent the most dramatic changes and, therefore, was selected as a model for further investigations into the mechanism of this conformational change. Herein we report the use of two-dimensional ROA correlation analysis applying synchronous, autocorrelation, and moving windows approaches in order to understand the conformational transitions in HSA as a function of DMSO concentration. Our results indicate that the destabilization of native alpha-helix starts at DMSO concentrations as little as 20% in water (v/v), with the transition to PPII helix being complete at similar to 80% DMSO. These results clearly indicate that any protein preparation containing relatively low concentrations of DMSO should consider possible disruptions in alpha-helical domains. (C) 2014 Wiley Periodicals, Inc.

Item Type:
Journal Article
Journal or Publication Title:
Chirality
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/3000/3004
Subjects:
ID Code:
71927
Deposited By:
Deposited On:
29 Nov 2014 00:05
Refereed?:
Yes
Published?:
Published
Last Modified:
05 Aug 2020 03:05