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- W2029125623 abstract "In order to investigate the structure-activity relationships between the hydrophobicity, differences in the number of positive charged amino acids and D-amino acids as well as their action mechanism with different bio-membranes, we designed and synthesized two sets of 12-mer model peptides originating from an amphiphilic antimicrobial model peptide and a D-amino acid-containing non-amphiphilic peptide. The introduction of D-amino acid in peptides led not only to decreases in the hydrophobicity, helical content, and hemolytic activity, but to an increase in the antimicrobial activity against Gram-positive and -negative bacteria. The relative peptide hydrophobicity was estimated in terms of the peptide elution time, expressed by linear trifluoroacetic acid (TFA)-water to TFA-acetonitrile gradients on C18 reverse-phase high-performance liquid chromatography (RP-HPLC). The retention behavior of model peptides on RP-HPLC is correlated with the activity and selectivity for mammalian cells, Gram-positive and -ne..." @default.
- W2029125623 created "2016-06-24" @default.
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- W2029125623 date "2000-10-01" @default.
- W2029125623 modified "2023-09-26" @default.
- W2029125623 title "The Effect of<b>D</b>-Amino Acid-Containing Basic Peptides with Different Hydrophobicity on the Antimicrobial and Cytotoxic Activity" @default.
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- W2029125623 doi "https://doi.org/10.1246/bcsj.73.2363" @default.
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