Purification and characterization of a novel antifungal protein with antiproliferation and anti-HIV-1 reverse transcriptase activities from Peganum harmala seeds.
Acta Biochim Biophys Sin (Shanghai)
; 45(2): 87-94, 2013 Feb.
Article
em En
| MEDLINE
| ID: mdl-23165744
ABSTRACT
A novel antifungal protein, designated as PHP, was isolated from the seeds of Peganum harmala, by cationic exchange chromatography on Resource S column and gel filtration on Sephadex 75 10/300 GL column. PHP was found to form a homodimer of about 16 kDa. Isoelectric focusing polyacrylamide gel electrophoresis analysis showed that the isoelectric point of PHP was â¼8.4. The N-terminal 20-amino acid sequence of PHP, ITCPQVTQSLAPCVPYLISG, resembles the non-specific lipid transfer proteins in certain plants. PHP exhibited lipid-binding activity. Furthermore, PHP exerted antifungal activity against Alternaria alternate, Penicillium degitatum, Rhizopus stuolonifer, and Magnaporthe grisea, and its antifungal activity was stable in the temperature range 4-60°C, and in the pH range 4-10. It inhibited the mycelial growth in A. alternate, P. degitatum, R. stuolonifer, and M. grisea with 50% inhibitory concentration (IC(50)) of 1.5, 37.5, 8.44, and 12.19 µM, respectively. PHP was also able to inhibit the proliferation of esophagus carcinoma (Eca-109), cervical carcinoma (HeLa), gastric carcinoma (MGC-7), and melanoma (B16) cells with IC(50) of 0.7, 2.74, 3.13, and 1.47 µM, respectively. Moreover, PHP significantly inhibited HIV-1 reverse transcriptase (RT) with an IC(50) of 1.26 µM. It did not have hemagglutinating and antibacterial activities. In conclusion, a novel antifungal protein with antiproliferation and anti-HIV-1 RT activities was obtained from P. harmala seeds.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
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Sementes
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Peganum
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Proliferação de Células
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Transcriptase Reversa do HIV
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Antifúngicos
Limite:
Humans
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article