Linked Life Data

18029121

Source:http://linkedlifedata.com/resource/pubmed/id/18029121

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2008-2-11
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-5173
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
351
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-60
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin.
pubmed:affiliation
School of Chemical Biology and Pharmaceutical Sciences, Capital Medical University, Beijing 100069, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't