Related Experiment Video
Updated: Jan 23, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
The Vast Structural Diversity of Antimicrobial Peptides
Johannes Koehbach1, David J Craik1
1Institute for Molecular Bioscience, The University of Queensland, 4072 Brisbane, QLD, Australia.
Abstract:
Antimicrobial peptides (AMPs) occur in all kingdoms of life and are integral to host defense. They have diverse structures and target a variety of organisms, both by nonspecific membrane interactions and via specific targets. Here we discuss the structures of AMPs from the four main classes currently recognized - that is, peptides with (i) α-helical, (ii) β-sheet, (iii) αβ, or (iv) non-αβ elements - as well as the growing pool of complex topologies including various post-translational modifications (PTMs). We propose to group these latter peptides into a fifth class of AMPs. Such peptides exhibit high stability and amenability to chemical engineering, making them of interest for the development of novel antimicrobial agents. Advances and challenges in the development of these peptides towards therapeutic leads are presented.
More Related Videos
Related Concept Videos
Peptide Bonds
Antimicrobial Effectiveness
Diversity of Archaea I
Diversity of Archaea II
Diversity of Protists I
Diversity of Protists II

