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Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds
- Source :
-
Peptides . Dec2008, Vol. 29 Issue 12, p2110-2117. 8p. - Publication Year :
- 2008
-
Abstract
- 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]
Details
- Language :
- English
- ISSN :
- 01969781
- Volume :
- 29
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Peptides
- Publication Type :
- Academic Journal
- Accession number :
- 35324541
- Full Text :
- https://doi.org/10.1016/j.peptides.2008.08.007