alexa Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin.
Chemistry

Chemistry

Medicinal Chemistry

Author(s): Wang N, Ye L, Yan F, Xu R

Abstract Share this page

Abstract Interaction between azelnidipine and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and circular dichroism (CD). Azelnidipine effectively quenched the intrinsic fluorescence of BSA via a combination of static and dynamic quenching, forming azelnidipine-BSA complex with binding constant (Ka) of the order of 10(5). The thermodynamic parameters obtained from van't Hoff equation revealed that both Delta H degrees and DeltaS degrees were negative, that is, -49.77 kJ mol(-1) and -64.47 J mol(-1)K(-1), respectively, suggesting that the binding is mainly driven by the enthalpy and hydrogen bonding plays major role in stabilizing azelnidipine-BSA complex. The binding of azelnidipine to BSA leads to changes in the conformation of BSA according to synchronous fluorescence spectra and CD data. The presence of metal ion decreases the binding constant of azelnidipine-BSA complex. This article was published in Int J Pharm and referenced in Medicinal Chemistry

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords