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Describes the purification and some properties of novel antimicrobial peptides (AMP) from Fagopyrum esculentum, which have a potent and wide antimicrobial activity against various pathogens. Methods used for purification; Concentration of peptides required for 50 percent inhibition of the growth of plant pathogenic fungi and Gram-positive and -negative bacteria.

Abstract: Novel antimicrobial peptides (AMP), designated Cy-AMP1, Cy-AMP2, and Cy-AMP3, were purified from seeds of the cycad (Cycas revoluta) by a CM cellulofine column, ion-exchange HPLC on SP COSMOGEL, and reverse-phase HPLC. They had molecular masses of 4583.2Da, 4568.9Da and 9275.8Da, respectively, by MALDI–TOF MS analysis. Half of the amino acid residues of Cy-AMP1 and Cy-AMP2 were cysteine, glycine and proline, and their sequences were similar. The sequence of Cy-AMP3 showed high homology to various lipid transfer proteins. For Cy-AMP1 and Cy-AMP2, the concentrations of peptides required for 50% inhibition (IC50) of the growth of plant pathogenic fungi, Gram-positive and Gram-negative bacteria were 7.0–8.9μg/ml. The Cy-AMP3 had weak antimicrobial activity. The structural and antimicrobial characteristics of Cy-AMP1 and Cy-AMP2 indicated that they are a novel type of antimicrobial peptide belonging to a plant defensin family. [Copyright &y& Elsevier]

Describes the purification and properties of two novel chitin-binding antimicrobial peptides from Tulipa gesneriana L. using chitin affinity chromatography. Characteristic properties of antimicrobial peptides; Antimicrobial activity of these two antimicrobial peptides against various pathogenic microorganisms; Function of antimicrobial peptides as self-defense against infection by various harmful pathogens.