Journal
PEPTIDES
Volume 29, Issue 12, Pages 2110-2117Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2008.08.007
Keywords
Cycas revoluta; Antimicrobial activity; Chitin binding domain; nsLTP; Plant defensin
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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 4583.2 Da, 4568.9 Da and 9275.8 Da, 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 7.0-8.9 mu g/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. (c) 2008 Elsevier Inc. All rights reserved.
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