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Antimicrobial β‐Peptides and α‐Peptoids
Author(s) -
Godballe Troels,
Nilsson Line L.,
Petersen Pernille D.,
Jenssen Håvard
Publication year - 2011
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2010.01067.x
Subject(s) - antimicrobial , antimicrobial peptides , drug , drug discovery , computational biology , metabolic stability , drug development , chemistry , pharmacology , combinatorial chemistry , biology , biochemistry , microbiology and biotechnology , in vitro
The field of drug discovery and development has seen tremendous activity over the past decade to better tackle the increasing occurrence of drug‐resistant bacterial infections and to alleviate some of the pressure we put on the last‐resort drugs on the market. One of the new and promising drug candidates is derived from naturally occurring antimicrobial peptides. However, despite promising results in early‐stage clinical trials, these molecules have faced some difficulties securing FDA approval, which can be linked to their poor metabolic stability. Hence, mimetics of these antimicrobial peptides have been suggested as new templates for antibacterial compound design, because these mimetics are resistant against degradation by proteases. This review will discuss the structural features of two different types of mimetics, β‐peptides and α‐peptoids, in relation to their antibacterial activity and conclude on their potential as new candidates for bacterial intervention.