37051-23-3Relevant articles and documents
CASPASE INHIBITORS AND METHODS OF USE THEREOF
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Paragraph 00303, (2020/09/19)
Provided herein are compounds of formula (I), compositions comprising the compounds and method of treating various diseases with the compounds and compositions.
Synthesis and biological evaluation of boron peptide analogues of Belactosin C as proteasome inhibitors
Nakamura, Hiroyuki,Watanabe, Mizuyoshi,Ban, Hyun Seung,Nabeyama, Wataru,Asai, Akira
scheme or table, p. 3220 - 3224 (2010/04/05)
A series of boron peptides 11, 13, 15 and 17 were designed and synthesized as proteasome inhibitors based on the structure of Belactosin C. Matteson homologation was a key step in the synthesis of the boron peptides. Compounds 11a and 13 showed significant inhibition of 20S proteasome chymotrypsin-like (β5) activity (IC50 = 0.28 and 0.51 μM, respectively). Furthermore, like PS-341, compound 11a increased the G2/M cell distribution. A biparametric cytofluorimetric analysis with FITC-labeled annexin V and propidium iodide showed induction of apoptosis by compound 11a at >1 μM concentrations of compound.
Synthesis of Peptide Analogues of Prothrombin Precursor Sequence 5-9. Substrate Specificity of Vitamin K Dependent Carboxylase
Rich, Daniel H.,Lehrman, S. Russ,Kawai, Megumi
, p. 706 - 711 (2007/10/02)
Thirty-five analogues of Phe-Leu-Glu-Glu-Leu, the pentapeptide sequence 5-9 of bovine prothrombin precursor, were synthesized and assayed as potential substrates or inhibitors of rat liver vitamin K dependent carboxylase.Carboxylation of substrate was determined by measuring the incorporation of carbon-14 labeled bicarbonate into product.Changes in substrate carboxylation produced by changing peptide chain length, amino acid chirality, or the distance seperating the peptide chain backbone from the carboxyl group were measured.The data suggest that the carboxylase carboxylates L-glutamic acid residues and does not carboxylate L-aspartic acid, L-homoglutamic acid, glutamine, or D-glutamic acid residues; tri- through pentapeptides are better substrates than mono- or bis(amino acid) derivatives, and hydrophobic groups added to the N-terminus can produce better substrates for the enzyme.None of the synthetic substrates is carboxylated as effectively as the endogenous protein substrates for the enzyme.The effect of structure on additional parameters affecting carboxylation is discussed.