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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.)

Selective DMSO-induced conformational changes in proteins from Raman optical activity

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Author(s):
Batista, Andrea N. L. [1, 2, 3] ; Batista, Jr., Joao M. [1, 2, 3] ; Bolzani, Vanderlan S. [3] ; Furlan, Maysa [3] ; Blanch, Ewan W. [1, 2]
Total Authors: 5
Affiliation:
[1] Univ Manchester, Manchester Inst Biotechnol, Manchester M1 7DN, Lancs - England
[2] Univ Manchester, Fac Life Sci, Manchester M1 7DN, Lancs - England
[3] Univ Estadual Paulista UNESP, Dept Quim Organ, BR-14800900 Araraquara - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Physical Chemistry Chemical Physics; v. 15, n. 46, p. 20147-20152, 2013.
Web of Science Citations: 29
Abstract

The function of a protein is determined by its structure, which is intrinsically related to its solvent environment. Based on this paradigm, there has been a great deal of interest in the role that nonaqueous solvents play in regulating protein structure, with some debate in the literature regarding dimethyl sulfoxide (DMSO). Thus, in this work we have used Raman and Raman optical activity (ROA) spectroscopies to investigate conclusively the changes induced by DMSO in the secondary structure of an array of proteins including human serum albumin (highly alpha-helical), bovine alpha-lactalbumin (mainly alpha-helical), bovine ribonuclease A (containing both alpha-helix and beta-sheet), bovine beta-lactoglobulin (mainly beta-sheet), and bovine alpha-casein (disordered). Our results clearly demonstrate that 100% DMSO solutions destabilize alpha-helices completely, converting them into the poly(L-proline) II (PPII) helix conformation. However, low concentrations of DMSO (10% v/v) were found to have little effect on the structure of even the most helical protein, human serum albumin. In the case of alpha-casein, the natively unfolded protein rich in PPII helix was converted into a further disordered structure when dissolved in pure DMSO. By contrast, beta-sheets remained mostly unaffected regardless of DMSO concentration. While providing new insights into protein structure in organic solvents, this work reinforces the capability of vibrational optical activity to assess conformations of biomolecules in conditions not accessible to other techniques, such as X-ray crystallography and NMR. (AU)

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
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: 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: 11/22339-4 - Chiroptical methods for the characterization of micro- and macromolecules from natural sources
Grantee:João Marcos Batista Junior
Support type: Scholarships in Brazil - Post-Doctorate