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.

journal_name

Amino Acids

journal_title

Amino acids

authors

Falciani C,Lozzi L,Scali S,Brunetti J,Bracci L,Pini A

doi

10.1007/s00726-014-1686-2

subject

Has Abstract

pub_date

2014-05-01 00:00:00

pages

1403-7

issue

5

eissn

0939-4451

issn

1438-2199

journal_volume

46

pub_type

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