Linked Life Data

20538509

Source:http://linkedlifedata.com/resource/pubmed/id/20538509

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-7-12
pubmed:abstractText
The interactions between 3,4-dihydropyrimidin-2(1H)-ones (DHPM) and bovine serum albumin (BSA) were investigated by fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The experimental results showed that all DHPM could form complexes with BSA. Static quenching and non-radiation energy transfer are the main reasons leading to the fluorescence quenching. The binding constants (K(A)) and the number of binding sites (n) were calculated. According to Förster theory of non-radiation energy transfer, the binding distances (r) between BSA and DHPM are less than 7 nm. The relationship between different aryl groups in pyrimidine ring and the binding ability of DHPM with BSA is preliminarily discussed. Moreover, the synchronous fluorescence spectra indicated that the conformation of BSA has not been changed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1873-3557
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Spectroscopic studies on the interactions between 3,4-dihydropyrimidin-2(1H)-ones and bovine serum albumin.
pubmed:affiliation
Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't