These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Study of the interaction between doxepin hydrochloride and bovine serum albumin by spectroscopic techniques.
    Author: Kandagal PB, Seetharamappa J, Ashoka S, Shaikh SM, Manjunatha DH.
    Journal: Int J Biol Macromol; 2006 Nov 15; 39(4-5):234-9. PubMed ID: 16678251.
    Abstract:
    The binding of doxepin hydrochloride (DH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-vis absorption and circular dichroism) techniques. The binding parameters have been evaluated by fluorescence quenching method. The thermodynamic parameters, Delta H major, Delta S major, and Delta G major calculated at different temperatures indicated that the hydrogen bond and hydrophobic forces played a major role in the interaction of DH with BSA. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (DH) was evaluated and found to be 2.7 nm. Spectral results observed showed that the binding of DH to BSA induced conformational changes in BSA. The effect of common ions on the binding of DH to BSA was also examined.
    [Abstract] [Full Text] [Related] [New Search]