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
Falciani, C., Lozzi, L., Scali, S., Brunetti, J., Bracci, L., Pini, A. (2014). Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase. AMINO ACIDS, 46(5), 1403-1407 [10.1007/s00726-014-1686-2].
Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase
FALCIANI, CHIARA;LOZZI, LUISA;SCALI, SILVIA;BRUNETTI, JLENIA;BRACCI, LUISA;PINI, ALESSANDRO
2014-01-01
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
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https://hdl.handle.net/11365/45849
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