Structure-function study of cathelicidin-derived bovine antimicrobial peptide BMAP-28 : design of its cell-selective analogs by amino acid substitutions in the heptad repeat sequences
Although BMAP-28 is a potent cathelicidin-derived bovine antimicrobial peptide, its cytotoxic activity against the human and other mammalian cells is of concern for converting it into a novel antimicrobial drug. We have identified a short leucine and isoleucine zipper sequences at the N- and C-terminals of BMAP-28, respectively. To understand the possible role of these structural elements in BMAP-