ArticleThe Biochemical journal1993
Peptide glyoxals: a novel class of inhibitor for serine and cysteine proteinases.
Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Microarray Selection of Cooperative Peptides for Modulating Enzyme Activities.Microarrays (Basel, Switzerland) · 2017Article
- A new lysine derived glyoxal inhibitor of trypsin, its properties and utilization for studying the stabilization of tetrahedral adducts by trypsin.Biochemistry and biophysics reports · 2016Article
- Quantifying tetrahedral adduct formation and stabilization in the cysteine and the serine proteases.Biochimica et biophysica acta · 2015Article
- A 13C-NMR study of the inhibition of papain by a dipeptide-glyoxal inhibitor.The Biochemical journal · 2002Article
- 13C-NMR study of the inhibition of delta-chymotrypsin by a tripeptide-glyoxal inhibitor.The Biochemical journal · 2002Article
- Peptidyl inverse esters of p-methoxybenzoic acid: a novel class of potent inactivator of the serine proteases.The Biochemical journal · 1997Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A series of novel synthetic dipeptides, containing a C-terminal glyoxal grouping (-COCHO), have been tested as inhibitors against typical members of the serine- and cysteine-proteinase families. For example, the sequences benzyloxycarbonyl (Cbz)-Pro-Phe-CHO (I) and Cbz-Phe-Ala-CHO (II), which fulfil the known primary and secondary specificity requirements of chymotrypsin and cathepsin B respectively, have been found to be potent reversible inhibitors of their respective target proteinase. Thus I was found to inhibit chymotrypsin with a Ki of approximately 0.8 microM, whereas II exhibits a Ki of approximately 80 nm against cathepsin B. These Ki values are some 10-fold and 3-fold lower than those reported for the corresponding peptide-aldehyde inhibitors of chymotrypsin and cathepsin B upon which the peptidyl-glyoxals were fashioned. Unexpectedly, the sequence Cbz-Pro-Ala-CHO, which was designed to inhibit elastase-like proteinases, exhibited no inhibitory activity towards porcine pancreatic elastase, even when used at concentrations as high as 200 microM.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.