Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities

J Biosci Bioeng. 2009 Sep;108(3):259-65. doi: 10.1016/j.jbiosc.2009.03.013.

Abstract

An 9.4-kDa antifungal peptide designated as campesin was isolated from seeds of the cabbage Brassica campestris. The isolation procedure involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono S, and gel filtration on Superdex 75 and Superdex Peptide. The peptide was adsorbed on the first three chromatographic media. It exerted an inhibitory action on mycelial growth including Fusarium oxysporum and Mycosphaerella arachidicola, with an IC(50) of 5.1 microM and 4.4 microM, respectively. The peptide was characterized by remarkable thermostability and pH stability. It inhibited proliferation of HepG2 and MCF cancer cells with an IC(50) of 6.4 microM and 1.8 microM, and the activity of HIV-1 reverse transcriptase with an IC(50) of 3.2 microM. It demonstrated lysolecithin binding activity.

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Ascomycota / metabolism
  • Brassica / metabolism*
  • Cell Line, Tumor
  • Chromatography, Affinity / methods*
  • Chromatography, Gel / methods
  • Chromatography, Ion Exchange / methods*
  • Fusarium / metabolism
  • HIV Integrase / metabolism
  • HIV Integrase Inhibitors / pharmacology
  • Humans
  • Inhibitory Concentration 50
  • Lecithins / chemistry
  • Peptides / chemistry
  • Plant Extracts / isolation & purification
  • Plant Extracts / pharmacology*
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology*
  • Reverse Transcriptase Inhibitors / pharmacology
  • Sepharose / chemistry

Substances

  • Antineoplastic Agents
  • HIV Integrase Inhibitors
  • Lecithins
  • Peptides
  • Plant Extracts
  • Plant Proteins
  • Reverse Transcriptase Inhibitors
  • campesin, Brassica campestris
  • Sepharose
  • HIV Integrase
  • p31 integrase protein, Human immunodeficiency virus 1