Abstract:
The emergence of drug resistant microorganisms poses a great worldwide threat and
created an immediate need for the development of novel antibiotics with different
mechanism of action. Microbial resistance to the antibiotics can affect any one
regardless of the gender, age and the country. In addition, microbial resistance to the
known antibiotics also imperil the progress in medical and health sciences. In this
context, the broad spectrum antimicrobial activity shown by the cationic host-defence
antimicrobial peptides (AMPs) have attracted considerable attention. Among various
types of host-defence peptides, helical motifs have been an active components of a
large family of cationic antimicrobial peptides. These peptides have shown excellent
antibacterial properties, however they suffer from non-specificity, higher hemolytic
activity and poor bioavailability. In this project, we have designed proteolytically stable
hybrid peptide 12-helical foldamers and investigated their antimicrobial activities
against various bacterial strains and also examine the haemolytic activity and their
proteolytic stability against serine protease trypsin. In comparison to α-peptide
counterpart, the hybrid peptide foldamers showed potent antibacterial activity and
showed increased stability against the protease trypsin.
