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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 26, Number 12
BKCSDE 26(12)
December 20, 2005 

Immobile Artificial Metalloproteases
Myoung-soon Kim, Junghun Suh*
Artificial enzymes, Artificial proteases, Metal catalysis, Peptide hydrolysis, Immobilized catalysts
Effective artificial metalloproteases have been designed by using cross-linked polystyrene as the backbone. Artificial active sites comprising Cu(II) complexes as the catalytic site and other metal centers or organic functionalities as binding sites were synthesized. The activity of Cu(II) centers for peptide hydrolysis was greatly enhanced on attachment to polystyrene. By placing binding sites in proximity to the catalytic centers, the ability to hydrolyze a variety of protein substrates at selected cleavage sites was improved. Thus far, the most advanced immobile artificial proteases have been obtained by attaching the aldehyde group in proximity to the Cu(II) complex of cyclen.
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