First isolation of an antifungal lipid transfer peptide from seeds of a Brassica species
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AbstractAn antifungal peptide with a molecular mass of 9412 and an N-terminal sequence exhibiting notable homology to those of lipid transfer proteins was isolated from seeds of the vegetable Brassica campestris. The purification protocol entailed ion exchange chromatography on Q-Sepharose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on a Superdex peptide column. The antifungal peptide was adsorbed on Affi-gel blue gel and Mono S. It inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola with an IC50 value of 8.3 mu M and 4.5 mu M, respectively. It exhibited dose-dependent binding to lyso-a-lauroyl phosphatidylcholine. The present findings constitute the first report on a non-specific lipid transfer protein from the seeds of a Brassica species. (c) 2007 Elsevier Inc. All rights reserved.
All Author(s) ListLin P, Xia LX, Ng TB
Journal namePeptides
Detailed descriptionTo ORKTS: DOI: 10.1016/j.peptides.2007.06.028
Year2007
Month8
Day1
Volume Number28
Issue Number8
PublisherELSEVIER SCIENCE INC
Pages1514 - 1519
ISSN0196-9781
eISSN1873-5169
LanguagesEnglish-United Kingdom
Keywordsantifungal non-specific lipid transfer protein; Brassica campestris; isolation; seeds
Web of Science Subject CategoriesBiochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Pharmacology & Pharmacy; PHARMACOLOGY & PHARMACY

Last updated on 2020-29-06 at 02:23