Cell Selectivity and Anti-inflammatory Activity of a Novel Tritrpticin Analog Containing Homo-tryptophan Peptoid Residues

摘要

Tritrpticin (TP), a member of the cathelicidin family, is a 13-amino-acid antimicrobial peptide (AMP) with a unique amino acid sequence (VRRFPWWWPFLRR) found in porcine leukocytes. TP has a high proportion of Arg (30%) and Trp (23%) residues. It forms a tritryptophan motif in the center of the peptide. Like indolicidin, it is classified into the group of Trp/Arg-rich AMPs. The solution structure of TP bound to sodium dodecyl sulfate (SDS) micelles was determined by the nuclear magnetic resonance (NMR) study. TP adopts an amphipathic turn-turn structure, with the Trp residues clustered together and inserted in the hydrophobic core of the micelle. TP has a broad spectrum of antimicrobial activity against Gram-positive and Gram-negative bacteria, as well as some fungi.1 Due to its short length and broad spectrum of antimicrobial activity, TP is a promising candidate for the development of antimicrobial drugs. The primary problem associated with peptide antimicrobial drug development is its lack of cell selectivity, the ability to distinguish pathogen cell against host cell, and one solution to overcome this is via incorporation of peptoid residues into the peptide.