Abstract
L-Threonine 2 was converted in seven steps into the protected aminomercaptoalcohol 8, a threonine mimic. This compound 8 was coupled to various oligopeptides to produce two different tetrapeptide analogues, for example, 11 and 17, which were shown to inhibit the Sortase enzymes (SrtA and SrtB) via covalent attachment of the thiol groups of 11 and 17 to the catalytically active cysteine residue of the Sortase enzymes.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aminoacyltransferases / antagonists & inhibitors*
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Aminoacyltransferases / metabolism*
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / metabolism*
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Butanols / chemical synthesis*
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Butanols / chemistry
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Butanols / pharmacology*
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Chromatography, High Pressure Liquid
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Cysteine Endopeptidases
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Molecular Structure
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Threonine / analogs & derivatives*
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Threonine / chemistry
Substances
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(2R,3S) 3-amino-4-mercapto-2-butanol
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Bacterial Proteins
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Butanols
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Enzyme Inhibitors
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Threonine
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Aminoacyltransferases
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sortase A
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Cysteine Endopeptidases