Abstract

The complex formed due to the interaction of the amphiphilic betablocker acebutolol with fibrinogen in a buffer solution (50mN glycine, pH of 8.5) has been investigated using a multipronged physicochemical approach. Differential scanning calorimetry measurements of the complexes have shown no reversibility of thermal denaturation as indicated by the three observed peaks and the opposite role that acebutolol plays in the folding different domains of the fibrinogen molecule and the stability of such domains. While circular dichroism measurements have revealed that interaction of acebutolol with fibrinogen affects the protein secondary structure to a different extent depending on the temperature and drug concentration, dynamic light scattering analysis showed evidence for protein aggregation mainly to tetramers and dimers.

Links

Publisher Full Text

Authors

Hassan N, Ruso JM, Somasundaran P

Institution

Soft Matter and Molecular Biophysics Group, Department of Applied Physics University of Santiago de Compostela, Campus Vida s/n, 15782, Santiago de Compostela, Spain.

Source

Colloids and surfaces. B, Biointerfaces 82:2 2011 Feb 1 pg 581-7

MeSH

Acebutolol
Animals
Buffers
Calorimetry, Differential Scanning
Cattle
Chemistry, Physical
Circular Dichroism
Dimerization
Fibrinogen
Glycine
Hydrogen-Ion Concentration
Light
Models, Chemical
Protein Folding
Scattering, Radiation

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21071185