The creation of new antimicrobial agents is a significant area of research needed to be
examined due to the era of antimicrobial resistance. Various microbial products are being studied
to combat this issue. One approach to tackle this problem is the use of antimicrobial peptides
(AMPs) which are the main focus of this study. However, using AMPs as antimicrobial medication
is hindered due to their potential toxic and hemolytic activity. This study will analyze the AMP
indolicidin which is known to have exceptional antimicrobial activity. Although a wide variety of
microbes are susceptible to indolicidin, it would make a poor pharmaceutical due to its high
hemolytic activity. To counter this, different derivatives of indolicidin will be examined that have
tryptophan amino acid residues replaced with alanine residues in an attempt to reduce hemolytic
properties, while also maintaining bioactivity. In this study, the indolicidin derivatives Δ4,8, Δ4,9,
Δ6,11, and Δ8,11 underwent antibiotic sensitivity testing to inspect their potential therapeutic use.
The cytotoxicity properties of the peptides was also analyzed via a hemolytic and
apoptotic/necrosis assay.
