Effect of hydrophobic chains on peptide antimicrobial and endotoxin-neutralizing activities

摘要

A plethora of human pathogens are now resistant to all clinically relevant antibiotics.This is causing a crisis in the treatment and management of infectious diseases and it presents a clear danger to future public health.In addition,septic shock resulting from bacterial infection remains a frequent cause of death,in particular in intensive care units.Gram-negative bacteria in particular contain lipopolysaccharides(or LPS)in their envelope,which are the most potent elicitors of this response known.As for antimicrobial activity,both hydrophobic and electrostatic interactions play a crucial role in a peptide LPS-neutralizing activity.Thus,using a series of analogs of a lactoferrin fragment(FQWQRNIRKVR),we have investigated how alteration or enhancement of such interactions affects a peptide antimicrobial and LPS-neutralizing activities.