Isolation and biochemical characterization of an antifungal peptide from Amaranthus hypochondriacus seeds.
An antifungal peptide, Ay-AMP, was isolated from Amaranthus hypochondriacus seeds by acidic extraction and then purified by reverse-phase high-pressure liquid chromatography. The molecular mass of this peptide, as determined by mass spectrometry, is 3184 Da. The peptide belongs to the superfamily of chitin-binding proteins, containing a single cysteine/glycine-rich chitin-binding domain, and it was found that Ay-AMP degrades chitin. Ay-AMP inhibits the growth, at very low doses, of different pathogenic fungi, such as Candida albicans, Trichoderma sp., Fusarium solani, Penicillium chrysogenum, Geotrichum candidum, Aspergillus candidus, Aspergillus schraceus, and Alternaria alternata. Ay-AMP is very resistant to the effect of proteases and heating; however, it showed an antagonistic effect with CaCl2 and KCl.
Rivillas-Acevedo
Lina A
LA
Departamento de Bioquímica, Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, Delegación Coyoacán C.P. 04510, México D.F., México.
Soriano-García
Manuel
M
D027721:Amaranthus / Q000737:chemistry*; D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D002352:Carrier Proteins; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000378:metabolism; D005659:Fungicides, Industrial / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D012639:Seeds / Q000737:chemistry*
D023181:Antimicrobial Cationic Peptides; C526151:Ay-AMP peptide; D002352:Carrier Proteins; D005659:Fungicides, Industrial; D010455:Peptides; D010940:Plant Proteins; D002686:Chitin; D002688:Chitinases