The Synthesis of Azapeptidomimetic β-Lactam Molecules as Potential Protease Inhibitors-Reference-Cited by-同舟云学术

The Synthesis of Azapeptidomimetic β-Lactam Molecules as Potential Protease Inhibitors

Published:2002-11-16 Issue:25 Volume:67 Page:8962-8969
ISSN:0022-3263
Container-title:The Journal of Organic Chemistry
language:en
Short-container-title:J. Org. Chem.

Author:

Malachowski William P.¹,Tie Chenyang¹,Wang Katherine¹,Broadrup Robert L.¹

Affiliation:

1. Department of Chemistry and Physics, The University of New England, Biddeford, Maine 04005, and Department of Chemistry, Bryn Mawr College, Bryn Mawr, Pennsylvania 19010-2899

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jo026280d

Reference67 articles.

1. Molecular Recognition of Protein−Ligand Complexes: Applications to Drug Design

2. Prime and nonprime refers to terminology originally proposed by I. Schechter and A. Berger (Biochem. Biophys. Res. Commun.1967,27, 157). The prime amino acids in a protease substrate extend in the carboxy terminal direction from the scissile bond starting with P1‘. The nonprime residues extend from the scissile bond in the amino terminal direction beginning with P1. The subsites in the enzyme associated with each amino acid position are denoted with S, e.g. S1‘ or S1.

3. On the size of the active site in proteases. I. Papain

4. On the size of the active site in proteases II. Carboxypeptidase-A

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