RT Journal Article
T1 A spectroscopic analysis of the interaction between MEGA10 and Concanavalin A
A1 Molina-Bolívar, José Antonio
A1 Carnero-Ruiz, Cristóbal
A1 Galisteo González, Francisco
A1 Aguilera Garrido, Aixa
A1 Gálvez Ruiz, María José
K1 Termodinámica
AB The binding of MEGA10 with Concanavalin A (Con A) at pH 7.4 and pH 5 have been studied using steady-stateand time-resolved fluorescence, dynamic light scattering (DLS) and Circular Dichroism(CD). Downward curvingStern-Volmer plots suggested the existence of tryptophan residues exposed in the protein surface and other tryptophansextensively buried within the protein. The major proportion of protein tryptophan groups are not involvedin MEGA10 interaction. The pH significantly influences the affinity of MEGA10 to Con A, with it beingstronger at pH 7.4 than at pH 5.0. It is inferred from the thermodynamic analysis of the binding constant dependencewithtemperature that van derWaals and hydrogen bonds are the predominant forces in the interaction ofMEGA10with lectin. In time-resolved fluorescence experiments, the decay curveswere well fitted to three exponentialpatterns. The mean lifetime at pH 7.4 systematically decreased with increasing MEGA10 concentration,whereas this parameter at pH 5 is practically constant, indicating greater protein structure alterations atpH 7.4 than at pH 5 after surfactant association, and they were corroborated by circular dichroismmeasurements.Anisotropy complementary studies detail that Con A undergoes motion restrictions because of the associationwith surfactant. The attachment of MEGA10 to Con A was confirmed by dynamic light scattering.
PB Elsevier
YR 2019
FD 2019
LK https://hdl.handle.net/10630/35606
UL https://hdl.handle.net/10630/35606
LA eng
NO J.A. Molina-Bolívar, C. Carnero Ruiz, F. Galisteo-González, A. Aguilera-Garrido, M.J. Gálvez-Ruiz, A spectroscopic analysis of the interaction between MEGA10 and Concanavalin A, Journal of Molecular Liquids, Volume 275, 2019, Pages 674-681, ISSN 0167-7322, https://doi.org/10.1016/j.molliq.2018.11.114
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 20 ene 2026