title: Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase.
abstract: M33 is a branched peptide currently under preclinical characterization for the development of a new antibacterial drug against gram-negative bacteria. Here, we report its pegylation at the C-terminus of the three-lysine-branching core and the resulting increase in stability to Pseudomonas aeruginosa elastase. This protease is a virulence factor that acts by destroying peptides of the native immune system. Peptide resistance to this protease is an important feature for M33-Peg activity against Pseudomonas.
authors: Dipartimento di Biotecnologie Mediche, Università di Siena, Siena, Italy.
authors: Chiara
authors: C
authors: Falciani
authors: Luisa
authors: L
authors: Lozzi
authors: Silvia
authors: S
authors: Scali
authors: Jlenia
authors: J
authors: Brunetti
authors: Luisa
authors: L
authors: Bracci
authors: Alessandro
authors: A
authors: Pini
mesh_terms: D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology*
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D011092:Polyethylene Glycols; D010196:Pancreatic Elastase