Virtually every living organism produces gene-encoded antimicrobial peptides
(AMPs) that provide an immediate defence against pathogen invasion. Many AMPs have
been isolated and used as antibiotics that are effective against multidrug-resistant bacteria.
Although encouraging, AMPs have such poor drug-like properties that their application for
clinical use is restricted. In turn, this has diverted research to the development of synthetic
molecules that retain the therapeutic efficacy of AMPs but are endowed with greater biological
stability and safety profiles. Most of the synthetic molecules, either based on a peptidic or
non-peptidic scaffold, have been designed to mimic the amphiphilic properties of native
AMPs, which are widely believed to be the key determinant of their antibacterial activity. In
this review, the structural, chemical and biophysical features that govern the biological activities
of various synthetic designs are discussed extensively. Recent innovative approaches
from the literature that exhibit novel concepts towards the development of new synthetic antibacterial
agents, including the engineered delivery platform incorporated with AMP mimetics,
are also emphasised.
Keywords: Antimicrobial peptides, synthetic mimics, antibacterial, amphiphilic properties, multidrug-resistant bacteria,
peptide, polymer, peptidomimetics.
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