Abstract
An 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 IC(50) value of 8.3 microM and 4.5 microM, respectively. It exhibited dose-dependent binding to lyso-alpha-lauroyl phosphatidylcholine. The present findings constitute the first report on a non-specific lipid transfer protein from the seeds of a Brassica species.
MeSH terms
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Amino Acid Sequence
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Antifungal Agents / chemistry
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Antifungal Agents / isolation & purification*
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Antifungal Agents / metabolism
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Antifungal Agents / pharmacology
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Antigens, Plant / genetics
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Antigens, Plant / isolation & purification*
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Antigens, Plant / metabolism
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Antigens, Plant / pharmacology
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Antimicrobial Cationic Peptides / genetics
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Antimicrobial Cationic Peptides / isolation & purification
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Antimicrobial Cationic Peptides / metabolism
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Antimicrobial Cationic Peptides / pharmacology
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Ascomycota / drug effects
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Brassica / chemistry*
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Brassica / genetics
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Carrier Proteins / genetics
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Carrier Proteins / isolation & purification*
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Carrier Proteins / metabolism
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Carrier Proteins / pharmacology
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Chromatography, Ion Exchange
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Fusarium / drug effects
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Lysophosphatidylcholines / metabolism
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Molecular Weight
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Plant Proteins / genetics
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Plant Proteins / isolation & purification*
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Plant Proteins / metabolism
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Plant Proteins / pharmacology
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Seeds / chemistry
Substances
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Antifungal Agents
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Antigens, Plant
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Antimicrobial Cationic Peptides
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Carrier Proteins
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Lysophosphatidylcholines
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Plant Proteins
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lipid transfer proteins, plant
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3-dodecanoylpropanediol-1-phosphorylcholine