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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007623,
umls-concept:C0007634,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0030956,
umls-concept:C0035654,
umls-concept:C0085493,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0521009,
umls-concept:C0599104,
umls-concept:C0887819,
umls-concept:C1167622,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1709634
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pubmed:issue |
1
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pubmed:dateCreated |
1989-2-6
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pubmed:abstractText |
Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cell wall have been developed to probe the details of the binding between ristocetin and N-acetylated peptides. The correlation equations indicate that (1) the binding is stronger for peptides in which the side chain of the C-terminal amino acid has a large molar refractivity (MR) value, (2) the binding is weaker for peptides with polar than for those with nonpolar C-terminal side chains, (3) the N-terminal amino acid in N-Ac dipeptides contributes 12 times that of the C-terminal amino acid to binding affinity, and (4) the interactions between ristocetin and the N-terminal amino acid of N-acetyl tripeptides appear to be much weaker than those with the first two amino acids.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-2623
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
84-93
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2909749-Acetylation,
pubmed-meshheading:2909749-Binding, Competitive,
pubmed-meshheading:2909749-Cell Wall,
pubmed-meshheading:2909749-Chemical Phenomena,
pubmed-meshheading:2909749-Chemistry,
pubmed-meshheading:2909749-Iodine Radioisotopes,
pubmed-meshheading:2909749-Micrococcus,
pubmed-meshheading:2909749-Models, Molecular,
pubmed-meshheading:2909749-Oligopeptides,
pubmed-meshheading:2909749-Radioligand Assay,
pubmed-meshheading:2909749-Ristocetin,
pubmed-meshheading:2909749-Structure-Activity Relationship
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pubmed:year |
1989
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pubmed:articleTitle |
Inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cells by the peptides related to bacterial cell wall mucopeptide precursors: quantitative structure-activity relationships.
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pubmed:affiliation |
Pharmaceutical Products Division, Abbott Laboratories, Abbott Park, Illinois 60064.
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pubmed:publicationType |
Journal Article
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