Linked Life Data

9621417

Source:http://linkedlifedata.com/resource/pubmed/id/9621417

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-7-9
pubmed:abstractText
The interaction between drugs (tolbutamide (1), 1-butyl-3-(methylsulfonyl)urea (2)) and human serum albumin (3) was investigated by equilibrium dialysis and NMR spectroscopy. The binding of 1 and 2 to 3 was concluded to be hydrophobic and hydrophilic, respectively, on the basis of the dependence of the binding constants on temperature, ionic strength, and chain length of fatty acid added. In 1H-NMR spectra of 1, there were no significant shifts with change in concentration or addition of 3. The spin-lattice relaxation time (T1) and spin-spin relaxation rate (1/T2) of the respective protons of 1 were independent of concentration, but depended on the concentration of 3 added. The binding position was determined from the ratio of 1/T2 of 1 bound to 3 and free 1. 1 and 2 were found to bind to 3 through the tolyl group and sulfonylurea group, respectively. The binding property of 1 was considered to be governed by the competition between the hydrophobic effect of the tolyl group and the hydrophilic effect of the sulfonylurea group in the molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0009-2363
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
817-21
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Binding position of tolbutamide to human serum albumin.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Japan.
pubmed:publicationType
Journal Article