Amino Acids

, Volume 46, Issue 5, pp 1403–1407 | Cite as

Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase

  • Chiara Falciani
  • Luisa Lozzi
  • Silvia Scali
  • Jlenia Brunetti
  • Luisa Bracci
  • Alessandro Pini
Short Communication
First Online:
Received:
Accepted:

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.

Keywords

Antimicrobial peptides Branched peptides Pegylation Peg Elastase Peptide stability 
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Notes

Acknowledgments

This research was supported by the Italian Foundation for Cystic Fibrosis (Project FFC#12/2013). The authors thank Gian Maria Rossolini and Simona Pollini for MICs calculation.

Conflict of interest

The patents covering the intellectual property of peptide M33 are owned by or licensed to SetLance. Chiara Falciani, Alessandro Pini and Luisa Bracci are partners of SetLance.

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Copyright information

© Springer-Verlag Wien 2014

Authors and Affiliations

  • Chiara Falciani
    • 1
    • 2
  • Luisa Lozzi
    • 1
  • Silvia Scali
    • 1
  • Jlenia Brunetti
    • 1
  • Luisa Bracci
    • 1
    • 3
  • Alessandro Pini
    • 1
    • 3
  1. 1.Dipartimento di Biotecnologie MedicheUniversità di SienaSienaItaly
  2. 2.SetLance srl, Toscana Life SciencesSienaItaly
  3. 3.Azienda Ospedaliera Universitaria SeneseSienaItaly

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