Monolayer-controlled substrate selectivity using non-covalent enzyme-nanoparticle conjugates

ORGN 259

Rui Hong, rhong@chem.umass.edu, Department of Chemistry, University of Massachusetts Amherst, 710 N. Pleasant St., Amherst, MA 01003, Todd Emrick, Department of Polymer Science and Engineering, University of Massachusetts, Amherst, 120 Governors Drive, Amherst, MA 01003, and Vincent M. Rotello, rotello@chem.umass.edu, Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003.
Surface-functionalized nanoparticles provide versatile scaffolds for protein surface binding through multivalent electrostatic interactions. The monolayer of the nanoparticle can be tailored to not only control protein (chymotrypsin)-nanoparticle interactions, but also impact the enzyme-substrate interaction. The electrostatic attraction or repulsion between nanoparticle monolayer and substrates of different charges affects the local concentrations of substrates abound the monolayer periphery. The chemo-selectivity of chymotrypsin upon adsorption onto the nanoparticle surface is thus enhanced with substrates of very similar structure but different charges. These findings demonstrate that nanoparticle scaffolds can be used to control over protein function on a higher level than a simple “on/off' mode, providing access to novel biocatalyst conjugates.

 

Molecular Recognition and Materials
1:00 PM-4:40 PM, Monday, 29 August 2005 Washington DC Convention Center -- 201, Oral

Division of Organic Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005