AApeptides as Antimicrobial PeptidomimeticsSHRUTI PADHEEDr. Jianfeng CaiDepartment of Chemistry, University of South FloridaThe emergent resistance of bacteria against the conventional antibiotics has motivated the search fornovel antimicrobial agents. Nature abounds with a number of antimicrobial peptides that are a part of ourinnate immune system and protect us against a variety of pathogenic bacteria. While they are broadspectrumin their activity and show less drug-resistance induction, their intrinsic metabolic stability limitstheir potential therapeutic applications. Herein we describe the development of novel broad-spectrumbioactive antimicrobial peptidomimetics-AApeptides. AApeptides were designed based on chiral PNAbackbone. Substitution of the nucleobases yields AApeptides that are resistant to proteolysis and are capableof mimicking peptides. AApeptides showing antibacterial activity were prepared by synthesizing cationicamphipathic antibacterial peptide mimics of varying lengths. The therapeutic potential of theseAApeptides were accessed by conducting antibacterial assays against a series of both gram-positive andgram-negative bacteria. The toxicity of the AA-peptides was evaluated against human erythrocytes andthese AApeptides were found to be almost non-hemolytic up to 100 ug/ml.

AApeptides as antimicrobial peptidomimetics

241st National Meeting (2011)

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