Design of β-Lactams with Mechanism Based Nonantibacterial Activities

Title: Design of β-Lactams with Mechanism Based Nonantibacterial Activities

Volume: 10 Issue: 17

Author(s): Grigory Veinberg, Maxim Vorona, Irina Shestakova, Iveta Kanepe and Edmunds Lukevics

Affiliation:

Keywords: nonantibacterial activities, phospholipase a2, a-independent transacylase, synthetic

Abstract: The majority of nonantibacterial activities discovered for β-lactam derivatives during the last 15 years are based on their ability to form a stable covalent complex with nucleophile in the active site of enzymes regulating fundamental physiological processes in mammalian organism such as serine and cysteine proteases, LDL phospholipase A2, A-independent transacylase and some still indeciphered enzymes. Regulation of their catalytic activity both in vitro and in vivo by compounds designed on the cephalosporin, penicillin and 2-azetidinone base was successfully exploited in the treatment of inflammatory, respiratory, cardiovascular disorders, cancer and other pathologic processes. Availability of X-ray crystallographic data for target enzymes and computational molecular modelling in combination with wide possibilities of structural modifications for commercial natural and synthetic β-lactams and the chiral blocks allow to consider this class of organic compounds as a perspective source of mechanism based nonantibacterial drugs.

Cite this article as:

Veinberg Grigory, Vorona Maxim, Shestakova Irina, Kanepe Iveta and Lukevics Edmunds, Design of β-Lactams with Mechanism Based Nonantibacterial Activities, Current Medicinal Chemistry 2003; 10 (17) . https://dx.doi.org/10.2174/0929867033457089