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Use of β-Amino Acids in the Design of Substrate-Based Peptidase Inhibitors

Autor: Michael J. Lew, Patrick Perlmutter, Marie-Isabel Aguilar, K. M. Stewart, M. F. Harte, E. Boulos, S. B. Reeve, Silas Bond, M. U. Norman, R. A. Lew, A. I. Smith

Publikováno v: Peptides: The Wave of the Future ISBN: 9789401039055

s-Amino acids contain an extra carbon between the amino and carboxy-termini; this modification renders the adjacent peptide bond resistant to hydrolysis [1,2]. We hypothesize that substitution of the residues at the scissile bond with s-amino acids c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::76c507ec28d0f35235999fae26b2c889
https://doi.org/10.1007/978-94-010-0464-0_257

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Bradykinin analogues with beta-amino acid substitutions reveal subtle differences in substrate specificity between the endopeptidases EC 3.4.24.15 and EC 3.4.24.16

Autor: R A, Lew, E, Boulos, K M, Stewart, P, Perlmutter, M F, Harte, S, Bond, M I, Aguilar, A I, Smith

Publikováno v: Journal of peptide science : an official publication of the European Peptide Society. 6(9)

The closely related zinc metalloendopeptidases EC 3.4.24.15 (EP24.15) and EC 3.4.24.16 (EP24.16) cleave many common substrates, including bradykinin (BK). As such, there are few substrate-based inhibitors which are sufficiently selective to distingui

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::73f4969120f7dddf6f7a2aa6815500de
https://pubmed.ncbi.nlm.nih.gov/11016880

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