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Control of Substrate Selectivity Through Complexation and Release of α-Chymotrypsin from Gold Nanoparticle Surfaces

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Mixed monolayer protected gold clusters (MMPCs) functionalized with mercaptoundecanoic acid (MUA) are efficient inhibitors of α-chymotrypsin (ChT). The binding of the ChT to MUA functionalized gold nanoparticles (MUA-AuNP) was found to denature the protein; however this complexation is reversible upon the addition of suitable positively charged surfactants. In this contribution we demonstrate that the released ChT has substrate selectivity differing from native ChT, with substrates featuring an extended peptide sequence completely inactive with the refolded enzyme. This alteration in activity provides a potential means for engineering substrate specificity, as well as providing a benchmark for correct refolding.
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Keywords: ALPHA-CHYMOTRYPSIN; GOLD NANOPARTICLES; MMPCS; PROTEIN ACTIVITY; PROTEINS; SUBSTRATE SELECTIVITY

Document Type: Research Article

Publication date: September 1, 2005

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  • Journal of Biomedical Nanotechnology (JBN) is a peer-reviewed multidisciplinary journal providing broad coverage in all research areas focused on the applications of nanotechnology in medicine, drug delivery systems, infectious disease, biomedical sciences, biotechnology, and all other related fields of life sciences.
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