Binding of barley and wheat alpha-thionins to polysaccharides.
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.
Oita
S
S
Shikoku National Agricultural Experiment Station, Ministry of Agriculture, Forestry and Fisheries, Zentsuji, Kagawa, Japan. oita@skk.affrc.go.jp
Ohnishi-Kameyama
M
M
Nagata
T
T
D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D002473:Cell Wall / Q000737:chemistry; D002686:Chitin / Q000032:analysis; D005936:Glucans; D001467:Hordeum / Q000737:chemistry*; D010940:Plant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D020539:Sequence Analysis, Protein; D014908:Triticum / Q000737:chemistry*
D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D005936:Glucans; D010940:Plant Proteins; D011134:Polysaccharides; C036092:hordothionin protein, Hordeum vulgare; D002686:Chitin; C008247:laminaran