Antimicrobial beta-peptides and beta-hairpins represented by the Gellman group
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Dr. Gellman has done extensive research to understand the intricate relationship between β-peptide structure and function. This thesis reviews the literature by the Gellman group, particularly on 12-helical β-peptides, 14-helical β-peptides, and β-Hairpins. The goal is to assess closely the relationship between conformational stability and antimicrobial potency of β-peptides. Literature based on interaction of 12-helical and 14-helical β-peptides, with liposomal membranes is reviewed to develop a perspective on the mechanism of antimicrobial action of β-peptides, Low hemolytic activity emerges as a remarkable feature of the β-peptides studied. A section is devoted to appraise literature on synthetic β-hairpins that adopt β-sheet conformation. These are designed as synthetic analogues of naturally occurring Protegrin 1 (PG-1). β-Hairpins lack cysteine residues present in PG-1 but still display antimicrobial activity. The analysis of structure-activity relationship studies helps to gain insight on the connections between β-sheet conformations and antimicrobial activity.