PMID: 10434050Aug 6, 1999Paper

Identification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein

Biochimica Et Biophysica Acta
Isidra Recio, S Visser

Abstract

Two distinct domains with antibacterial activity were isolated from a peptic hydrolysate of bovine alpha(s2)-casein. The digested alpha(s2)-casein was fractionated by cation-exchange chromatography, after which the peptides in the two active fractions obtained were separated by high-performance liquid chromatography and sequenced by electrospray-ionization tandem mass spectrometry. The major component in each active fraction, f(183-207) and f(164-179), was further purified and the antibacterial activity of these components was tested against several microorganisms. Depending on the target bacterial strain, these peptides exhibited minimum inhibitory concentrations between 8 and 99 microM. Peptide f(183-207) exhibited a consistently higher antibacterial activity than f(164-179), although both peptides showed a comparable hemolytic effect. A method of in situ enzymatic hydrolysis on a cation-exchange membrane to obtain a fraction enriched in the most active antibacterial domain is presented. The antibacterial and hemolytic activities are discussed in relation to the structure and hydrophobicity of the peptides.

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Citations

Apr 28, 2001·Biochimica Et Biophysica Acta·A PellegriniP Hunziker
Oct 11, 2003·Biotechnology Advances·A F Kolb
Jun 25, 2013·Applied and Environmental Microbiology·Avelino Alvarez-OrdóñezColin Hill
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