A serine protease inhibitor from hemolymph of green mussel, Perna viridis

Bioorganic & Medicinal Chemistry Letters
2008.0

Abstract

Bioactivity guided fractions of cell-free hemolymph of bacterially challenged marine mussel, Perna viridis led to the isolation of a novel quaternary alkaloid 1, which was identified by its spectral data. The isolated molecule 1 has been found to be a potent serine protease inhibitor (SPI) showing IC(50) and K(i) values of 102.5 and 97.1-104.68 microM, respectively. The E(t)/K(i) value of SPI is 6.3, whereas E(t)/K(m) value is 1.04. The Van't Hoff analysis showed that the value of K(i) decreases with increase in temperature, and the binding of the inhibitor is entropically driven.

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