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Conformational Analysis of a Synthetic Antimicrobial Peptide in Water and Membrane-Mimicking Solvents: A Molecular Dynamics Simulation Study

  • Sandro L. ForniliEmail author
  • Rita Pizzi
  • Davide Rebeccani
Article

Abstract

We have investigated structural and dynamic properties of the synthetic peptide hlF1-11 (GRRRSVQWCA, i.e., the first 11 N-terminal amino acids of the human lactoferrin protein) in water, 250 mM NaCl solution, 50% (V/V) water–trifluoroethanol mixture, and in the membrane mimetic 4:4:1 methanol–chloroform–water mixture. For comparison, we have also performed analogous simulations for the biologically inactive control peptide featuring Ala substitutions in the 2, 3, 6 and 9 positions of the hlF1-11 sequence. Statistical analyses of the trajectories indicate that only in the membrane-mimicking medium hlF1-11 adopts preferentially a conformation suitable to interact effectively with the membrane. In this conformation the peptide cationic region is rather flexible and elongated, while the C-terminal hydrophobic moiety appears as a more rigid hairpin-shaped loop approximately perpendicular to the cationic region. No such conformation is statistically relevant for the control peptide.

Keywords

Antimicrobial peptides Human lactoferrin Molecular dynamics simulation Membrane-mimicking solvents 

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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Sandro L. Fornili
    • 1
    • 2
    • 3
    Email author
  • Rita Pizzi
    • 1
  • Davide Rebeccani
    • 1
  1. 1.Dipartimento di Tecnologie dell’InformazioneUniversità di MilanoCremaItaly
  2. 2.CISIMilanItaly
  3. 3.CNISMRomeItaly

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