Amino Acids

, Volume 40, Issue 1, pp 61–68

Amino acid substitutions in an alpha-helical antimicrobial arachnid peptide affect its chemical properties and biological activity towards pathogenic bacteria but improves its therapeutic index

Authors

  • A. Rodríguez
    • Departamento de Medicina Molecular y Bioprocesos, Instituto de BiotecnologíaUniversidad Nacional Autónoma de México, UNAM
  • E. Villegas
    • Centro de Investigación en BiotecnologíaUniversidad Autónoma del Estado de Morelos, Av. Universidad 1001
  • H. Satake
    • Suntory Institute for Bioorganic Research
  • L. D. Possani
    • Departamento de Medicina Molecular y Bioprocesos, Instituto de BiotecnologíaUniversidad Nacional Autónoma de México, UNAM
    • Departamento de Medicina Molecular y Bioprocesos, Instituto de BiotecnologíaUniversidad Nacional Autónoma de México, UNAM
Original Article

DOI: 10.1007/s00726-009-0449-y

Cite this article as:
Rodríguez, A., Villegas, E., Satake, H. et al. Amino Acids (2011) 40: 61. doi:10.1007/s00726-009-0449-y

Abstract

Four variants of the highly hemolytic antimicrobial peptide Pin2 were chemically synthesized with the aim to investigate the role of the proline residue in this peptide, by replacing it with the motif glycine-valine-glycine [GVG], which was found to confer low hemolytic activity in a spider antimicrobial peptide. The proline residue in position 14 of Pin2 was substituted by [V], [GV], [VG] and [GVG]. Only the peptide variant with the proline substituted for [GVG] was less hemolytic compared to that of all other variants. The peptide variant [GVG] kept its antimicrobial activity in Muller–Hilton agar diffusion assays, whereas the other three variants were less effective. However, all Pin2 antimicrobial peptide variants, were active when challenged against a Gram-positive bacteria in Muller–Hilton broth assays suggesting that chemical properties of the antimicrobial peptides such as hydrophobicity is an important indication for antimicrobial activity in semi-solid environments.

Keywords

Antimicrobial peptide Arachnid, pandinin 2 Peptide synthesis S. aureus

Abbreviations

CD

Circular dichroism

OD

Optical density

Oxki2

Oxypinin 2

Pin2

Pandinin 2

TFA

Trifluoroacetic acid

TFE

Trifluoroethanol

MIC

Minimum inhibitory concentration

Copyright information

© Springer-Verlag 2009