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Antibacterial Activity of Lactophoricin, a Synthetic 23-Residues Peptide Derived from the Sequence of Bovine Milk Component-3 of Proteose Peptone

¹ Laboratoire des Biosciences de l’Aliment, UC INRA 885, Université Henri Poincaré, Nancy-1, BP 239, 54506 Vanduvre-lès-Nancy Cedex, France
² Laboratoire Universitaire de Microbiologie Appliquée de Quimper, EA 2651, 6 rue de l’Université, 29334 Quimper, France

Corresponding author: S. Campagna; e-mail: campagna{at}scbiol.uhp-nancy.fr.

A synthetic peptide of 23 residues corresponding to the carboxyterminal 113 to 135 region of component-3 of proteose peptone (PP3) has been investigated with regard to its antibacterial properties. This cationic amphipathic peptide that we refer to as lactophoricin, displayed a growth-inhibitory activity against both gram-positive and gram-negative bacteria. For most of the strains tested, bacterial growth was observed in the presence of lactophoricin except for Streptococcus thermophilus. In that case, lactophoricin exhibited a minimum inhibitory concentration of 10 µM and a minimum lethal concentration of 20 µM. No hemolysis of human red blood cells was detected for peptide concentrations between 2 to 200 µM, indicating that lactophoricin would be noncytotoxic when used in this concentration range.

Key Words: bovine milk • component-3 of proteose peptone • antimicrobial activity • amphipathic peptide

Abbreviation key: IC₅₀ = half inhibitory concentration, MIC = minimal inhibitory concentration, MLC = minimum lethal concentration, NMR = nuclear magnetic resonance, PP3 = component-3 of proteose peptone, RBC = red blood cell

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