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- W2015388564 abstract "Analogs of the antithrombin peptide hirudin54–65 with C-terminal modifications have been synthesized in order to examine the requirements for α-thrombin inhibition. The C-terminal residue, Gln65, could be replaced with -amino acids or amino alcohols with neutral or charged hydrophilic side chains without greatly affecting the peptide's antithrombin potency as determined by inhibition of thrombin-induced clot formation in human plasma . Derivatives with or -amino carboxamides at position 65-had significantly reduced potency, but still retained activity. Deletion of residue 65 with conversion of residue 64 to the amide or alcohol derivative resulted in a three-fold loss of potency. In addition to these results the solid-phase synthesis of peptide alcohols via direct displacement of p-nitrobenzhydrylideneisonitroso resin attached peptides with the desired C-terminal amino alcohol is reported." @default.
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- W2015388564 title "C-Terminal peptide alcohol, acid and amide analogs of desulfato hirudin54–65 as antithrombin agents" @default.
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- W2015388564 doi "https://doi.org/10.1016/0049-3848(89)90090-x" @default.
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