5v1e
From Proteopedia
Suboptimization of a glycine rich peptide allows the combinatorial space exploration for designing novel antimicrobial peptides
Structural highlights
Publication Abstract from PubMedPlants are extensively used in traditional medicine, and several plant antimicrobial peptides have been described as potential alternatives to conventional antibiotics. However, after more than four decades of research no plant antimicrobial peptide is currently used for treating bacterial infections, due to their length, post-translational modifications or high dose requirement for a therapeutic effect . Here we report the design of antimicrobial peptides derived from a guava glycine-rich peptide using a genetic algorithm. This approach yields guavanin peptides, arginine-rich alpha-helical peptides that possess an unusual hydrophobic counterpart mainly composed of tyrosine residues. Guavanin 2 is characterized as a prototype peptide in terms of structure and activity. Nuclear magnetic resonance analysis indicates that the peptide adopts an alpha-helical structure in hydrophobic environments. Guavanin 2 is bactericidal at low concentrations, causing membrane disruption and triggering hyperpolarization. This computational approach for the exploration of natural products could be used to design effective peptide antibiotics. In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design.,Porto WF, Irazazabal L, Alves ESF, Ribeiro SM, Matos CO, Pires AS, Fensterseifer ICM, Miranda VJ, Haney EF, Humblot V, Torres MDT, Hancock REW, Liao LM, Ladram A, Lu TK, de la Fuente-Nunez C, Franco OL Nat Commun. 2018 Apr 16;9(1):1490. doi: 10.1038/s41467-018-03746-3. PMID:29662055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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