1. Isolation of a new trypsin inhibitor from the Faba bean (Vicia faba cv. Giza 843) with potential medicinal applications.
- Author
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Fang EF, Hassanien AA, Wong JH, Bah CS, Soliman SS, and Ng TB
- Subjects
- Amino Acid Sequence, Antineoplastic Agents chemistry, Antineoplastic Agents pharmacology, Cell Line, Tumor, Egypt, HIV Reverse Transcriptase chemistry, Humans, Molecular Sequence Data, Plant Proteins pharmacology, Reverse Transcriptase Inhibitors chemistry, Trypsin Inhibitors pharmacology, Plant Proteins chemistry, Seeds chemistry, Trypsin Inhibitors chemistry, Vicia faba chemistry
- Abstract
A new 15-kDa Bowman-Birk type trypsin inhibitor (termed VFTI-G1) was isolated from the seeds of Faba bean (Vicia faba cv. Giza 843) using cation exchange chromatography on an SP-Sepharose column, anion exchange chromatography on Q-Sepharose and Mono Q columns, and finally size exclusion chromatography on a Superdex 75 column. VFTI-G1 manifested significant antiproteolytic activity against trypsin (5761 BAEE units/mg, K(i) 20.4 × 10(-9) M), but only a slight chymotrypsin inhibitory activity (< 10 BTEE units/mg). The suitable environment to sustain its trypsin inhibitory activity was at temperatures below 60 °C and at pH 7. Its trypsin inhibitory activity was inhibited by the reducing agent dithiothreitol in a dose-dependent manner, indicating the significance of intact disulfide bonds to the trypsin inhibitory activity. It inhibited HIV-1 reverse transcriptase (RT) activity with an IC(50) of about 0.76 µM. Furthermore, VFTI-G1 showed specific antiproliferative activity toward HepG2 hepatoma cells by inducing chromatin condensation and cell apoptosis. The HIV-1 RT inhibitory activity of VFTI-G1 and its specific antiproliferative activity toward Hep G2 cells may find medical applications.
- Published
- 2011
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