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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

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Author(s):
Batista, Andrea N. L. [1, 2, 3] ; Batista, Jr., Joao M. [1, 2, 3] ; Ashton, Lorna [2, 4] ; Bolzani, Vanderlan S. [1] ; Furlan, Maysa [1] ; Blanch, Ewan W. [2, 3]
Total Authors: 6
Affiliation:
[1] Univ Estadual Paulista UNESP, Inst Quim, Dept Quim Organ, BR-14800060 Araraquara, SP - Brazil
[2] Univ Manchester, Manchester Inst Biotechnol, Manchester, Lancs - England
[3] Univ Manchester, Fac Life Sci, Manchester, Lancs - England
[4] Univ Manchester, Sch Chem, Manchester, Lancs - England
Total Affiliations: 4
Document type: Journal article
Source: Chirality; v. 26, n. 9, SI, p. 497-501, SEP 2014.
Web of Science Citations: 10
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. (AU)

FAPESP's process: 13/07600-3 - CIBFar - Center for Innovation in Biodiversity and Drug Discovery
Grantee:Glaucius Oliva
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 12/16484-4 - Raman optical activity: an innovative tool for protein structural analysis
Grantee:Andrea Nastri de Luca Batista
Support type: Scholarships abroad - Research Internship - Post-doctor
FAPESP's process: 12/13739-1 - Vibrational optical activity as a probe to molecular chirality
Grantee:João Marcos Batista Junior
Support type: Scholarships abroad - Research Internship - Post-doctor