Assessment of interactions between four proteins and benzothiazole derivatives by DSC and CD

Hassan, Natalia; Verdes, Pedro V.; Ruso, Juan M.

Abstract

The thermal denaturation of ovalbumin, lysozyme, myoglobin and fibrinogen at different BTS concentrations have been investigated using differential scanning calorimetry (DSC) and circular dichroism (CD) spectroscopy. Thermodynamic parameters: melting temperatures (T-m), calorimetric enthalpy (Delta H), van't Hoff enthalpy (Delta H-v) were obtained for all the systems under study. Thermal denaturation of the four proteins was completely irreversible. Changes in the protein conformation due to the adsorption of BTS molecules have been monitored by using UV-CD spectra. Greater changes in a-helical contents correspond with the BTS higher concentrations. The lysozyme denaturation temperature increases at low concentrations BTS indicating that BTS acts as a structure stabilizer; meanwhile it acts as a destabilizer at higher concentrations in all the proteins studied. The major effect is observed in the case of myoglobin, the protein with the highest alpha-helical secondary structure (75%). (C) 2010 Elsevier Ltd. All rights reserved.

Más información

Título de la Revista: JOURNAL OF CHEMICAL THERMODYNAMICS
Volumen: 43
Asunto: 3
Editorial: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Fecha de publicación: 2011-01-01
Página de inicio: 399
Página final: 404
DOI/URL:

10.1016/j.jct.2010.10.015

Identificador: 10.1016/j.jct.2010.10.015
Notas: ISI