Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2002-9-23
pubmed:abstractText
Electrostatic interactions have been proposed as a potentially important force for anesthetics and protein binding but have not yet been tested directly. In the present study, we used wild-type human serum albumin (HSA) and specific site-directed mutants as a native protein model to investigate the role of electrostatic interactions in halothane binding. Structural geometry analysis of the HSA-halothane complex predicted an absence of significant electrostatic interactions, and direct binding (tryptophan fluorescence and zonal elution chromatography) and stability experiments (hydrogen exchange) confirmed that loss of charge in the binding sites, by charged to uncharged mutations and by changing ionic strength of the buffer, generally increased both regional (tryptophan region) and global halothane/HSA affinity. The results indicate that electrostatic interactions (full charges) either do not contribute or diminish halothane binding to HSA, leaving only the more general hydrophobic and van der Waals forces as the major contributors to the binding interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36373-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12118010-Amides, pubmed-meshheading:12118010-Anesthetics, Inhalation, pubmed-meshheading:12118010-Binding Sites, pubmed-meshheading:12118010-Cloning, Molecular, pubmed-meshheading:12118010-DNA, Complementary, pubmed-meshheading:12118010-Halothane, pubmed-meshheading:12118010-Humans, pubmed-meshheading:12118010-Hydrogen, pubmed-meshheading:12118010-Inhibitory Concentration 50, pubmed-meshheading:12118010-Ions, pubmed-meshheading:12118010-Liver, pubmed-meshheading:12118010-Models, Molecular, pubmed-meshheading:12118010-Mutagenesis, Site-Directed, pubmed-meshheading:12118010-Mutation, pubmed-meshheading:12118010-Protein Binding, pubmed-meshheading:12118010-Protein Structure, Tertiary, pubmed-meshheading:12118010-Recombinant Proteins, pubmed-meshheading:12118010-Serum Albumin, pubmed-meshheading:12118010-Spectrometry, Fluorescence, pubmed-meshheading:12118010-Static Electricity, pubmed-meshheading:12118010-Time Factors, pubmed-meshheading:12118010-Tritium, pubmed-meshheading:12118010-Tryptophan
pubmed:year
2002
pubmed:articleTitle
The role of electrostatic interactions in human serum albumin binding and stabilization by halothane.
pubmed:affiliation
Department of Anesthesia, University of Pennsylvania, Philadelphia, Pennsylvania 19104-4283, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.