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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 25, Number 12
BKCSDE 25(12)
December 20, 2004 

Artificial Metalloproteases with Broad Substrate Selectivity Constructed on Polystyrene
Eun Hwa Ko, Junghun Suh*
Artificial protease, Metalloprotease, Substrate selectivity, Cu(II)-cyclen, Polystyrene
Although the proteolytic activity of the Cu(II) complex of cyclen (Cyc) is greatly enhanced upon attachment to a cross-linked polystyrene (PS), the Cu(II)Cyc-containing PS derivatives reported previously hydrolyzed only a very limited number of proteins. The PS-based artificial metalloproteases can overcome thermal, mechanical, and chemical instabilities of natural proteases, but the narrow substrate selectivity of the artificial metalloproteases limits their industrial application. In the present study, artificial metalloproteases exhibiting broad substrate selectivity were synthesized by attaching Cu(II)Cyc to a PS derivative using linkers with various structures in an attempt to facilitate the interaction of various protein substrates with the PS surface. The new artificial metalloproteases hydrolyzed all of the four protein substrates (albumin, myoglobin, γ-globulin, and lysozyme) examined, manifesting kcat/Km values of 28-1500 h?1M?1 at 50 oC. The improvement in substrate selectivity is attributed to steric and/or polar interaction between the bound protein and the PS surface as well as the hydrophobicity of the microenvironment of the catalytic centers.
1917 - 1923
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