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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1981-10-25
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pubmed:abstractText |
A series of analogues relating to the NH2-terminal region of the fibrin alpha chain, i.e., Gly-Pro-Arg-Pro, were prepared by stepwise solid-phase synthesis, and their abilities to inhibit fibrin polymerization and to prolong thrombin-initiated clotting time were evaluated. Among the analogues systematically modified at different positions, replacement of the NH2-terminal three residues of Gly-Pro-Arg-Pro by either chlorambucil, p-nitrophenyl-L-alanine, or p-aminophenyl-L-alanine gave inactive compounds in the thrombin time assay, whereas similar substitution or extension of the COOH terminus produced the highly active analogues Gly-Pro-Arg-Phe(4-NH2), 22%; Gly-Pro-Arg-Pro-Phe(4-NO2), and Gly-Pro-Arg-Pro-Phe(4-NH2), 105%; relative to Gly-Pro-Arg-Pro = 100% in the fibrin polymerization inhibitory assay. As potential photoaffinity labeling probes, analogues containing a nitrophenylalanine residue in position 4 or 5 underwent photolysis under the experimental photoactivation conditions. As a potential alkylating probe, Chl-Pro-Arg-Pro was selectively effective in inhibiting thrombin amidolysis and fibrin polymerization. In the latter assay, Chl-Pro-Arg-Pro was approximately 20 times more potent than Gly-Pro-Arg-Pro in inhibiting fibrin aggregation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticoagulants,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2623
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
322-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7265118-Alkylation,
pubmed-meshheading:7265118-Anticoagulants,
pubmed-meshheading:7265118-Binding Sites,
pubmed-meshheading:7265118-Fibrin,
pubmed-meshheading:7265118-Humans,
pubmed-meshheading:7265118-Peptides,
pubmed-meshheading:7265118-Photolysis,
pubmed-meshheading:7265118-Polymers,
pubmed-meshheading:7265118-Structure-Activity Relationship,
pubmed-meshheading:7265118-Thrombin
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pubmed:year |
1981
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pubmed:articleTitle |
Fibrin Polymerization. 1. Alkylating peptide inhibitors of fibrin polymerization.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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