title: Archetypal tryptophan-rich antimicrobial peptides: properties and applications.
abstract: Drug-resistant microorganisms ('superbugs') present a serious challenge to the success of antimicrobial treatments. Subsequently, there is a crucial need for novel bio-control agents. Many antimicrobial peptides (AMPs) show a broad-spectrum activity against bacteria, fungi or viruses and are strong candidates to complement or substitute current antimicrobial agents. Some AMPs are also effective against protozoa or cancer cells. The tryptophan (Trp)-rich peptides (TRPs) are a subset of AMPs that display potent antimicrobial activity, credited to the unique biochemical properties of tryptophan that allow it to insert into biological membranes. Further, many Trp-rich AMPs cross bacterial membranes without compromising their integrity and act intracellularly, suggesting interactions with nucleic acids and enzymes. In this work, we overview some archetypal TRPs derived from natural sources, i.e., indolicidin, tritrpticin and lactoferricin, summarising their biochemical properties, structures, antimicrobial activities, mechanistic studies and potential applications.
authors.affiliation: Faculty of Science, Engineering and Technology, Swinburne University of Technology, PO Box 218, Hawthorn, VIC, 3122, Australia.
authors.forename: Nadin
authors.initials: N
authors.lastname: Shagaghi
authors.affiliation: Faculty of Science, Engineering and Technology, Swinburne University of Technology, PO Box 218, Hawthorn, VIC, 3122, Australia.
authors.forename: Enzo A
authors.initials: EA
authors.lastname: Palombo
authors.affiliation: Faculty of Science, Engineering and Technology, Swinburne University of Technology, PO Box 218, Hawthorn, VIC, 3122, Australia.
authors.forename: Andrew H A
authors.initials: AH
authors.lastname: Clayton
authors.affiliation: Faculty of Science, Engineering and Technology, Swinburne University of Technology, PO Box 218, Hawthorn, VIC, 3122, Australia. mbhave@swin.edu.au.
authors.forename: Mrinal
authors.initials: M
authors.lastname: Bhave
mesh_terms: D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D004352:Drug Resistance, Microbial; D006801:Humans; D007781:Lactoferrin / Q000737:chemistry / Q000494:pharmacology; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D014364:Tryptophan / Q000737:chemistry* / Q000494:pharmacology*
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; C402895:tritrpticin; C073143:indolicidin; C082171:lactoferricin B; D014364:Tryptophan; D007781:Lactoferrin
keywords: Antimicrobial agents; Antimicrobial peptides (AMP); Mechanisms of action; Trp-rich peptides (TRP); Tryptophan