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Molecular engineering of a small trypsin inhibitor based on the binding loop of horsegram seed Bowman-Birk inhibitor
Deepa G Muricken1, Lalitha R Gowda
1Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Council of Scientific and Industrial Research, Mysore, India.
Context:
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 K(i) (3.2 ± 0.17 × 10(-8) M) establishes a very high affinity to bovine trypsin. rTID inhibited human lung tryptase (IC(50) 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.
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