Journal
PHYTOMEDICINE
Volume 16, Issue 2-3, Pages 172-180Publisher
ELSEVIER GMBH
DOI: 10.1016/j.phymed.2008.12.025
Keywords
Antifungal protein; Passiflora edulis; beta-Lactoglobulin
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Funding
- CUHK Research Committee
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The intent was to isolate an antifungal protein from seeds of the passion fruit (Passiflora edulis) and to compare its characteristics with other antifungal proteins and bovine beta-lactoglobulin in view of its N-terminal amino acid sequence similarity to beta-lactoglobulin. The isolation procedure entailed ion-exchange chromatography on Q-Sepharose, hydrophobic interaction chromatography on Phenyl-Sepharose, ion-exchange chromatography on DEAE-cellulose, and FPLC-gel filtration on Superdex 75. The isolated 67-kDa protein, designated as passiflin, exhibited an N-terminal amino acid sequence closely resembling that of bovine beta-lactoglobulin. It is the first antifungal protein found to have a beta-lactoglobulin-like N-terminal sequence. Its dimeric nature is rarely found in antifungal proteins. It impeded mycelial growth in Rhizotonia solani with an IC50 of 16 mu M and potently inhibited proliferation of MCF-7 breast cancer cells with an IC50 of 15 mu M There was no cross-reactivity of passiflin with anti-beta-lactoglobulin antiserum. Intact P-lactoglobulin lacks antifungal and antiproliferative activities and is much smaller in molecular size than passiflin. However, it has been reported that hydrolyzed P-lactoglobulin shows antifungal activity. The data suggest that passiflin is distinct from beta-lactoglobulin. (C) 2009 Elsevier GmbH. All rights reserved.
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