A minimalist design approach to antimicrobial agents based on a thionin template.
Numerous studies have been devoted to the stabilization of secondary structure elements to improve receptor-ligand recognition. We report a novel application of this principle to create new antimicrobial agents using the highly folded thionin from Pyrularia puberaas a template. Non-native disulfide bonds have been used to induce two short linear segments of the protein into an amphipathic helix. The resulting 13- and 9-residue peptides are significantly more active than their linear counterparts and have an activity similar to that of native thionin.
Vila-Perelló
Miquel
M
Department of Experimental and Health Sciences, Pompeu Fabra University, E-08003 Barcelona, Spain.
Tognon
Sabrina
S
Sánchez-Vallet
Andrea
A
García-Olmedo
Francisco
F
Molina
Antonio
A
Andreu
David
D
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D000890:Anti-Infective Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D000935:Antifungal Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D002942:Circular Dichroism; D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; D010940:Plant Proteins; C044942:THI1 protein, Pyrularia pubera