A serine protease inhibitor from hemolymph of green mussel, Perna viridis
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 sub(50) and K sub(i) values of 102.5 and 97.1-104.68 mu M, respectively. The E sub(t)/K sub(i) value of SPI is 6.3, whereas E sub(t)/K sub(m) value is 1.04. The Van't Hoff analysis showed that the value of K sub(i) decreases with increase in temperature, and the binding of the inhibitor is entropically driven.
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