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 (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 the entropic factor to the complex formation. The formation of specific complexes of HMIQ3c1 with the kallikrein (K_D = 2.81 × 10^–8 М) and neutrophil elastase (K_D = 1.11 × 10^–7 М) indicates its anti-inflammatory activity and makes prospects to use the peptide as a potential therapeutic agent.

中文翻译：

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巨大的海葵异型海葵的Kunitz型肽的新目标。

摘要

使用表面等离振子共振方法研究了海葵巨大异形海葵的Kunitz型肽HMIQ3c1与几种丝氨酸蛋白酶（包括炎性蛋白酶）的相互作用。我们表明，HMIQ3c1形式足够强的复合物用胰蛋白酶（重组模拟ķ _d = 1.07×10 ^-9 М）和胰凝乳蛋白酶（ķ _d = 4.70×10 ^-8 М）。HMIQ3c1 /胰凝乳蛋白酶的热力学参数分析表明，熵因素对复合物的形成有重要作用。HMIQ3c1与激肽释放酶的特定复合物的形成（K _D = 2.81×10 ^–8М）和中性白细胞弹性蛋白酶（ķ _d = 1.11×10 ^-7 М）指示其抗炎活性并使得前景使用肽作为潜在的治疗剂。