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- Title
Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy.
- Authors
Batista, Andrea N. L.; Batista, João M.; Ashton, Lorna; Bolzani, Vanderlan S.; Furlan, Maysa; Blanch, Ewan W.
- Abstract
ABSTRACT Recent Raman and Raman optical activity (ROA) results have demonstrated that dimethyl sulfoxide (DMSO) induces the selective conversion of α-helix motifs into the poly(L-proline) II (PPII) helix conformation in an array of proteins, while β-sheets remain mostly unaffected. Human serum albumin (HSA), a highly α-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 α-helix starts at DMSO concentrations as little as 20% in water (v/v), with the transition to PPII helix being complete at ~80% DMSO. These results clearly indicate that any protein preparation containing relatively low concentrations of DMSO should consider possible disruptions in α-helical domains. Chirality 26:137-141, 2014. © 2014 Wiley Periodicals, Inc.
- Subjects
DIMETHYL sulfoxide; SERUM albumin; RAMAN spectroscopy; CONFORMATIONAL analysis; AUTOCORRELATION (Statistics)
- Publication
Chirality, 2014, Vol 26, Issue 9, p137
- ISSN
0899-0042
- Publication type
Article
- DOI
10.1002/chir.22351