Stabilization of chymotrypsin at the air-water interface

ORGN 477

Brian J Jordan, bjjordan@chem.umass.edu1, Rui Hong, rhong@chem.umass.edu2, Jason Hill3, Basar Gider4, and Vincent M. Rotello, rotello@chem.umass.edu1. (1) Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, (2) Department of Chemistry, University of Massachusetts Amherst, 710 N. Pleasant St., Amherst, MA 01003, (3) Department of Molecular and Cellular Biology, University of Massachusetts, 710 N. Pleasant St., Amherst, 01003, (4) Department of Chemistry, University of Massachusetts at Amherst, 710 N. Pleasant St., Amherst, MA 01003
Maintaining protein structure and function at the air-water interface is important in biotechnology. The ability to preserve the protein at the interface promotes technical advances in storage, handling, production methods, and surface applications. In our current research, we have demonstrated the stabilization of a-chymotrypsin (ChT) at the air-water interface by using a surface-active nanoparticle, AuTCOOH. Upon addition to a ChT solution, AuTCOOH binds electrostatically to the ChT, reducing the interfacial surface energy at the air-water interface. The AuTCOOH nanoparticle subsequently protects the ChT from hydrophobic protein-air interactions that would otherwise denature the protein. This protein stabilization process is demonstrated through Circular Dichroism (CD) and kinetic assays.

 

Bioorganic, Metal-Mediated Reactions, and Molecular Recognition
8:00 PM-10:00 PM, Tuesday, 30 August 2005 Washington DC Convention Center -- Hall A, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, 29 August 2005 Washington DC Convention Center -- Hall A, Sci-Mix

Division of Organic Chemistry

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