RT Journal Article
T1 Unfolding Pathway of a Globular Protein by Surfactants Monitored with Raman Optical Activity
A1 Nieto-Ortega, Belén
A1 Hierrezuelo-Osorio, José Manuel
A1 Carnero-Ruiz, Cristóbal
A1 López-Navarrete, Juan Teodomiro
A1 Casado-Cordón, Juan
A1 Ramírez-Aguilar, Francisco Javier
K1 Agentes tensioactivos
AB Protein denaturation by surfactants has received increased attention in the last years due to its implications in topics such as pharmaceutics, cosmetics, paints, or biotechnology. This phenomenon is highly dependent on the physicochemical (structural)properties of the denaturing agents. In this work, we have measured for the first time the Raman optical activity (ROA) of bovine serum albumin (BSA) in the presence of three surfactants (anionic, cationic, and neutral), which has allowed us to detect newspectroscopic insights of the protein−surfactant interaction that conventional Raman spectroscopy cannot. Our work proposes two new groups of ROA marker bands to explore the unfolding of BSA induced by surfactants, which are related to “polar” (amide Iand III modes) and “apolar” (methylene bending and phenyl breathing modes) protein sections. The appearance of the former groups is related to the initial attack of the surfactant, while the second groups relate to the hydrophobic unfolding.
PB ACS Publications
YR 2014
FD 2014
LK https://hdl.handle.net/10630/33827
UL https://hdl.handle.net/10630/33827
LA eng
NO Nieto-Ortega, B.; J.M. Hierrezuelo; C. Carnero Ruiz; Lopez-Navarrete, J.T.; Casado, J.; Ramirez, F.J. Unfolding Pathway of a Globular Protein by Surfactants Monitored with Raman Optical Activity. Journal of Physical Chemistry Letters (2014), 5 (1), pp. 8-13.
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 20 ene 2026