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Syntheses of antibacterial peptides,gramicidin S analogs and designed amphiphilic oligopeptides
Institution:1. Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, Saint Louis, MO, USA;2. Saint Louis University Liver Center, Saint Louis, MO, USA;3. Department of Chemistry, Brooklyn College, City University of New York, Brooklyn, NY, USA;4. PhD Program in Chemistry, The Graduate Center of the City University of New York, New York, NY, USA;1. Department of Material and Environmental Chemistry, Graduate School of Engineering, Utsunomiya University, 7-1-2 Yoto, Utsunomiya, Tochigi 321-8585, Japan;2. Creative Department of Innovation, Graduate School of Engineering, Utsunomiya University, 7-1-2 Yoto, Utsunomiya, Tochigi 321-8585, Japan
Abstract:In order to clarify the relationship between antimicrobial activity and peptide-structure, gramicidin S analogs and cationic α-helical model peptides were designed and synthesized. Introduction of cationic side chains in hydrophilic side of gramicidin S increased antimicrobial activity against Gram-negative bacteria. Amphiphilic structures of the α-helical peptides were found to be effective to show antimicrobial activities against Gram positive bacteria. Increase in number of cationic amino acid residues in the α-helical peptides caused appreciable antimicrobial activities against Gram-negative bacteria, however, induced lower activities against Gram-positive ones.
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