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Citation (#18):

Identification of two distinct antibacterial domains within the sequence of bovine alphas2-casein

Authors: Recio, I., Visser, S.

Journal: Biochimica et Biophysica Acta (BBA) - General Subjects 1999, 1428(2-3).

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Abstract

Two distinct domains with antibacterial activity were isolated from a peptic hydrolysate of bovine αs2-casein. The digested αs2-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(183207) and f(164179), 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 μM. Peptide f(183207) exhibited a consistently higher antibacterial activity than f(164179), 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.

Keywords: Antibacterial peptide; [alpha]s2-Casein; Electrospray mass spectrometry; Hydrolysis of membrane-bound protein

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