New Targets of Kunitz-Type Peptide from Sea Anemone Heteractis magnifica


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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.

About the authors

A. N. Kvetkina

Elyakov Pacific Institute of Bioorganic Chemistry,
Far East Branch, Russian Academy of Sciences

Author for correspondence.
Email: kvetkinaan@gmail.com
Russian Federation, Vladivostok, 690022

L. A. Kaluzhskiy

Orekhovich Institute of Biomedical Chemistry,
Russian Academy of Medical Sciences

Email: kvetkinaan@gmail.com
Russian Federation, Pogodinskaya ul. 10, Moscow, 119832

E. V. Leychenko

Elyakov Pacific Institute of Bioorganic Chemistry,
Far East Branch, Russian Academy of Sciences; Far East Federal University

Email: kvetkinaan@gmail.com
Russian Federation, Vladivostok, 690022; Vladivostok, 690022

M. P. Isaeva

Elyakov Pacific Institute of Bioorganic Chemistry,
Far East Branch, Russian Academy of Sciences

Email: kvetkinaan@gmail.com
Russian Federation, Vladivostok, 690022

A. S. Ivanov

Orekhovich Institute of Biomedical Chemistry,
Russian Academy of Medical Sciences

Email: kvetkinaan@gmail.com
Russian Federation, Pogodinskaya ul. 10, Moscow, 119832

E. P. Kozlovskaya

Elyakov Pacific Institute of Bioorganic Chemistry,
Far East Branch, Russian Academy of Sciences

Email: kvetkinaan@gmail.com
Russian Federation, Vladivostok, 690022

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