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
Full text not available from this repository.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.