Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
}
TY - JOUR
T1 - Investigation of DMSO-induced conformational transitions in human serum albumin using two-dimensional Raman optical activity spectroscopy
AU - Batista, Andrea N. L.
AU - Batista, Joao M.
AU - Ashton, Lorna
AU - Bolzani, Vanderlan S.
AU - Furlan, Maysa
AU - Blanch, Ewan W.
PY - 2014/9
Y1 - 2014/9
N2 - 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.
AB - 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.
KW - ROA
KW - 2DCOS
KW - HSA
KW - moving windows
KW - protein
KW - secondary structure
KW - PPII helix
KW - BOVINE ALPHA-LACTALBUMIN
KW - SEQUENTIAL ORDER
KW - PROTEINS
KW - HELIX
KW - LYSOZYME
KW - RULES
KW - STATE
U2 - 10.1002/chir.22351
DO - 10.1002/chir.22351
M3 - Journal article
VL - 26
SP - 497
EP - 501
JO - Chirality
JF - Chirality
SN - 0899-0042
IS - 9
ER -