| Joseph M. Simard1, Nicholas O. Fischer2, Ayush Verma3, Catherine M. Goodman3, and Vincent M Rotello4. (1) Department of Chemistry, University of Massachusetts-Amherst, 701 LGRT, 710 N. Pleasant St., Amherst, MA 01003, (2) Department of Chemisty, University of Massachusetts, Amherst, Lederle Graduate Research Tower, Room 701, 710 N. Pleasant St., Amherst, MA 01002, (3) Department of Chemistry, University of Massachusetts Amherst, 710 N. Pleasant St., Amherst, MA 01003, (4) Department of Chemistry, UMASS, 701 North Pleasant Street, Amherst, MA 01003 |
Protein surface recognition provides a powerful means for the regulation of protein activity. For sufficient surface binding to occur the recognition systems need to be of comparable size with a high degree of organization to provide a complementary surface for recognition. To date, research in this area has focused on large monomeric receptors, peptide, and polymer systems. Gold nanoparticles offer a particularly effective scaffold for protein surface recognition due to their comparable size, ease of fabrication, and ability to synthesize a wide variety of different systems with distinctive functionalities for recognition. In our current research, we have synthesized gold nanoparticles with different recognition elements that completely inhibit alpha-chymotrypsin at physiological levels. This introduces a new class of protein inhibitors, featuring a versatile platform for multivalent recognition.  |