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Biosci Biotechnol Biochem. 2000 May;64(5):958-64.

Binding of barley and wheat alpha-thionins to polysaccharides.

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Shikoku National Agricultural Experiment Station, Ministry of Agriculture, Forestry and Fisheries, Zentsuji, Kagawa, Japan.


An antimicrobial peptide termed BCP-2 was purified from barley grain by chitin-affinity treatment and HPLC. The results of amino acid analysis and mass spectrometry of BCP-2 indicate that the peptide is very similar to barley alpha-thionin. BCP-2 and wheat alpha1-thionin were also bound to beta-glucan but not to starch. The binding of BCP-2 to laminarin (beta-1,3-1,6-glucan) and laminarioligosaccharides was supported by fluorescence polarization data. This is the first report on the binding of alpha-thionins to polysaccharide containing chitin and beta-1,3-glucan, which construct fungal cell walls.

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