Abstract
The interaction of Kunitz-type peptide, HMIQ3c1, from the sea anemone Heteractis magnifica with several serine proteases, including inflammatory proteases, was investigated using the surface plasmon resonance approach. We showed that the recombinant analog of HMIQ3c1 forms sufficiently strong complexes with trypsin (KD = 1.07 × 10–9 М) and chymotrypsin (KD = 4.70 × 10–8 М). Analysis of thermodynamic parameters of HMIQ3c1/chymotrypsin revealed significant contribution of the entropic factor to the complex formation. The formation of specific complexes of HMIQ3c1 with the kallikrein (KD = 2.81 × 10–8 М) and neutrophil elastase (KD = 1.11 × 10–7 М) indicates its anti-inflammatory activity and makes prospects to use the peptide as a potential therapeutic agent.
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ACKNOWLEDGMENTS
The optical-biosensor analysis of intermolecular interactions was performed using the equipment of the “Human Proteome” Core Facility (Orekhovich Institute of Biomedical Chemistry).
Funding
The study was supported by the Basic Research Program for State Academies of Sciences for 2013–2020 (theme no. 0518-2018-0003 “Study of Pharmacological Targets of Biologically Active Compounds and Systems of Their Delivery to the Human Body”).
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Translated by M. Batrukova
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Kvetkina, A.N., Kaluzhskiy, L.A., Leychenko, E.V. et al. New Targets of Kunitz-Type Peptide from Sea Anemone Heteractis magnifica. Dokl Biochem Biophys 487, 260–263 (2019). https://doi.org/10.1134/S1607672919040033
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DOI: https://doi.org/10.1134/S1607672919040033