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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/51816
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dc.contributor.authorPearson, D.-
dc.contributor.authorAbell, A.-
dc.date.issued2008-
dc.identifier.citationARKIVOC, 2008; 2008(12):85-93-
dc.identifier.issn1551-7004-
dc.identifier.issn1551-7012-
dc.identifier.urihttp://hdl.handle.net/2440/51816-
dc.description.abstractThree new compounds (3-5) based on a dipeptide non-covalent inhibitor (1) of α-chymotrypsin have been synthesised and assayed against the serine protease α-chymotrypsin. The stability of the compounds to α-chymotrypsin catalysed hydrolysis has been measured. All three compounds were inactive with a retained stability to enzyme catalysed hydrolysis.-
dc.description.statementofresponsibilityDavid Pearson and Andrew D. Abell-
dc.language.isoen-
dc.publisherArkat USA, Inc.-
dc.source.urihttp://www.arkat-usa.org/arkivoc-journal/browse-arkivoc/2008/12/-
dc.subjectChymotrypsin-
dc.subjectenzyme inhibitors-
dc.subjectpeptidomimetics-
dc.subjectazobenzene-
dc.titleD-Leu-L-Phe-containing dipeptide inhibitors of -chymosrypsin- the role of the N- and C-termini in enzyme affinity-
dc.typeJournal article-
dc.identifier.doi10.3998/ark.5550190.0009.c10-
pubs.publication-statusPublished-
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]-
Appears in Collections:Aurora harvest
Chemistry and Physics publications

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