Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.

By D. I. Chan, E. Prenner, Hans J. Vogel. Biochimica et Biophysica Acta, 2006

1,005 citations recorded by the source corpus.

Antimicrobial peptides encompass a number of different classes, including those that are rich in a particular amino acid. An important subset are peptides rich in Arg and Trp residues, such as indolicidin and tritrpticin, that have broad and potent antimicrobial activity. The importance of these two amino acids for antimicrobial activity was highlighted through the screening of a complete combinatorial library of hexapeptides. These residues possess some crucial chemical properties that make them suitable components of antimicrobial peptides. Trp has a distinct preference for the interfacial region of lipid bilayers, while Arg residues endow the peptides with cationic charges and hydrogen bonding properties necessary for interaction with the abundant anionic components of bacterial membranes. In combination, these two residues are capable of participating in cation-pi interactions, thereby facilitating enhanced peptide-membrane interactions. Trp sidechains are also implicated in peptide and protein folding in aqueous solution, where they contribute by maintaining native and nonnative hydrophobic contacts. This has been observed for the antimicrobial peptide from human lactoferrin, possibly restraining the peptide structure in a suitable conformation to interact with the bacterial membrane. These unique properties make the Arg- and Trp-rich antimicrobial peptides highly active even at very short peptide lengths. Moreover, they lead to structures for membrane-mimetic bound peptides that go far beyond regular alpha-helices and beta-sheet structures. In this review, the structures of a number of different Trp- and Arg-rich antimicrobial peptides are examined and some of the major mechanistic studies are presented.

Subfields: Cellular and Molecular Neuroscience, Immunology, Microbiology

View Paper: https://www.semanticscholar.org/paper/38f2926868fadf46497ec28d0a7a6df60f2575c9

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Citations in the corpus

Self-assembled cationic peptide nanoparticles as an efficient antimicrobial agent. (2009, background): “, thus destabilizing the membrane based on the electroporation andsor sinking raft mode”
Cell‐penetrating peptides: 20 years later, where do we stand? (2013, background): “In addition, it was demonstrated that tryptophan residues are involved in membrane destabilization processes [108,109].”
Studies on anticancer activities of antimicrobial peptides. (2008, background): “An important set of AMPs, such as tritrpticin, lactoferricins and indolicidin, are rich in Trp and Arg residues [18].”
The Roles of Antimicrobial Peptides in Innate Host Defense (2009, background): “When stacked perpendicularly this shields Arg residues allowing them to make cation-π interactions with water, thus stabilizing their insertion into the membrane [73].”
From antimicrobial to anticancer peptides. A review (2013, background): “A review”
Antimicrobial peptides: The ancient arm of the human immune system (2010, background): “The 13-residue AMP contains 5 tryptophan residues (39%), thus displaying the highest tryptophan proportion ever seen in a peptide or protein.(37) Upon interaction with biological membranes indolicidin assumes a wedge- or boatshaped conformation with the hydrophobic tryptophan residues in the wedge’s”