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Molecular engineering of a small trypsin inhibitor based on the binding loop of horsegram seed Bowman-Birk inhibitor.

Deepa, G. Muricken and Lalitha, R. Gowda (2011) Molecular engineering of a small trypsin inhibitor based on the binding loop of horsegram seed Bowman-Birk inhibitor. Journal of Enzyme Inhibition and Medicinal Chemistry, 26 (4). 553-560 .

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Abstract

The Bowman-Birk inhibitors (BBIs) are currently investigated with renewed interest due to their therapeutic properties in cancer and other inflammatory disease treatment. The molecular mass of the BBI is a limitation, as sufficient amounts of the inhibitor do not reach the organs outside the gastrointestinal tract when administered orally. Method: The anti-tryptic domain of HGI-III of horsegram (Dolichos biflorus) was cloned using the vector pET-20b (+) and expressed in E. coli BL21 (DE3) pLysS. Results: Kinetic analysis of this anti-tryptic peptide (recombinant trypsin inhibitory domain (rTID)) reveals that it is a potent inhibitor of trypsin and human tryptase. The Ki (3.2 ± 0.17 × 10−8 M) establishes a very high affinity to bovine trypsin. rTID inhibited human lung tryptase (IC50 3.78 ± 0.23 × 10−7 M). The rTID is resistant to the digestive enzymes found in humans and animals. Conclusion: These properties propagate further research on the use of rTID as a therapeutic for cancer and other related inflammatory diseases.

Item Type: Article
Uncontrolled Keywords: Dolichos biflorus, recombinant trypsin inhibitor domain, protein expression, trypsin/tryptase inhibition, bioavailability
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Aug 2011 07:15
Last Modified: 08 Aug 2011 07:15
URI: http://ir.cftri.com/id/eprint/10423

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