Unbound MEDLINE

Mechanisms of fibrinogen-acebutolol interactions: Insights from DSC, CD and LS.

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