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Current Medicinal Chemistry - Anti-Infective Agents


ISSN (Print): 1568-0126
ISSN (Online): 1875-600X

Structure Activity Relationship Study and Recent Advances in the Design and Synthesis about Linear Antimicrobial Peptides

Author(s): Keun-Hyeung Lee

Volume 1, Issue 3, 2002

Page: [305 - 318] Pages: 14

DOI: 10.2174/1568012023354884

Price: $65


Numerous defense peptides (cationic antimicrobial peptides) were isolated from eukaryotic systems and their functions were studied. In spite of size, primary sequences, and structures, most of them shared common features. They preferentially bind to lipid membranes of microbes and increase permeability of lipid membranes as a primary mode of action. The characteristics of cationic antimicrobial peptide different from conventional antibiotics make themselves a candidate for novel antimicrobial agents. In this review, we will provide a general overview of linear antimicrobial peptides with emphasis on aspects such as structure, biological mode, and structural parameters for activity and selectivity in vitro. And this review will focus on recent design and synthesis of novel peptide analogs with enhanced stability and selectivity.

Keywords: antimicrobial peptide, cationic antimicrobial peptide, linear antimicrobial, cationic antimicrobial

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