Tuning hydrophobicity of highly cationic tetradecameric Gramicidin S analogues using adamantane amino acids.
Basic Information
ID: ALA1287679
Journal: Bioorg Med Chem
Title: Tuning hydrophobicity of highly cationic tetradecameric Gramicidin S analogues using adamantane amino acids.
Authors: Knijnenburg AD, Kapoerchan VV, Spalburg E, de Neeling AJ, Mars-Groenendijk RH, Noort D, van der Marel GA, Overkleeft HS, Overhand M.
Abstract: Ring extended Gramicidin S analogues containing adamantane amino acids and six cationic residues were designed and evaluated. Systematic replacement of the hydrophobic residues with adamantane amino acids resulted in a small set of compounds with varying amphipathic character. It was found that the amphipathicity of these compounds is correlated to their biological activity. Several bacterial strains including MRSA strains were shown to be killed by the novel peptides. The most potent antibacterial peptides are tetradecameric GS analogues containing six positives charges and two adamantane moieties.
CiteXplore: 20951594
DOI: 10.1016/j.bmc.2010.09.018
Patent ID: ┄