Generic placeholder image

Current Topics in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1568-0266
ISSN (Online): 1873-4294

Structural Consideration of Macrolide Antibiotics in Relation to the Ribosomal Interaction and Drug Design

Author(s): Hajime Takashima

Volume 3, Issue 9, 2003

Page: [991 - 999] Pages: 9

DOI: 10.2174/1568026033452177

Price: $65

Abstract

Macrolide antibiotics exert antimicrobial effects by binding to the peptidyl transferase center of the 50S subunit of bacterial ribosomes and inhibiting protein synthesis. Hence, the structure of macrolides and their interaction with bacterial ribosomes have been investigated in order to understand the structural mechanisms of macrolide-ribosome interaction. Most macrolides have been found tom adopt a common conformation both in crystal form and in solution, which is believed to play an important role for binding to bacterial ribosomes as well as representing bi-facial property essential for excellent biological functions of macrolides. Chemical footprinting and mutant analysis have offered topological information on macrolide-ribosome interaction at the nucleotide level. Recently, crystal structures of the 50S ribosomal subunit and the 50S subunit with macrolide antibiotics have been published. These crystal structures provide much structural information on macrolideribosome interaction at the atomic level and will enable structure-based drug design of novel macrolide antibiotics with potent activity against resistant strains.

Keywords: Macrolide Antibiotics, bi-facial, topological, footprinting


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy