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Matches in SemOpenAlex for { <https://semopenalex.org/work/W2027046501> ?p ?o ?g. }

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• W2027046501 abstract "The mechanism of proteolysis by serine proteases is a reasonably well-understood process. Typically, a histidine residue acting as a general base deprotonates the catalytic serine residue and the hydrolytic water molecule. We disclose here, the use of an unnatural d-amino acid as a strategic residue in P1 position, designed de novo based on the architecture of the protease catalytic site to impede the catalytic histidine residue at the stage of acyl-enzyme intermediate. Several probe molecules containing d-homoserine or its derivatives at P1 position are evaluated. Compounds 1, 6, and 8-10 produced up to 57% loss of activity against chymotrypsin. More potent and specific inhibitors could be designed with structure optimization as this strategy is completely general and can be used to design inhibitors against any serine or cysteine protease." @default.
• W2027046501 created "2016-06-24" @default.
• W2027046501 creator A5004904484 @default.
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• W2027046501 date "2006-01-01" @default.
• W2027046501 modified "2023-10-06" @default.
• W2027046501 title "Engineering d-amino acid containing novel protease inhibitors using catalytic site architecture" @default.
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• W2027046501 doi "https://doi.org/10.1016/j.bmc.2005.08.019" @default.
• W2027046501 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16198572" @default.
• W2027046501 hasPublicationYear "2006" @default.
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