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 α-thionin. BCP-2 and wheat α₁-thionin were also bound to β-glucan but not to starch. The binding of BCP-2 to laminarin (β-1,3-1,6-glucan) and laminarioligosaccharides was supported by fluorescence polarization data. This is the first report on the binding of α-thionins to polysaccharide containing chitin and β-1,3-glucan, which construct fungal cell walls.

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