New targets of Kunitz-type peptide from sea anemone Heteractis magnifica

The interaction of Kunitz-type peptide, HMIQ3c1, from sea anemone Heteractis magnifica with several serine proteases including inflammatory proteases was investigated using surface plasmon resonance approach. We showed that recombinant analog of HMIQ3c1 makes strong enough complexes with trypsin ( K D = 1,07 × 10 -9 М) and chymotrypsin ( K D = 4,70 × 10 -8 М). Analysis of thermodynamic parameters of HMIQ3c1/chymotrypsin revealed significant contribution of entropic factor in complex formation. The formation of specific complexes of HMIQ3c1 with neutrophil elastase ( K D = 1,11 × 10 -7 М) and kallikrein ( K D = 2,81 × 10 -8 М) indicates its anti-inflammatory activity and makes prospects to use the peptide as a potential therapeutic agent.