Electrochemical characterization of covalently immobilized ferritin

ANYL 128

Sean S. Casella, SSC4591@sru.edu, Chemistry, Slippery Rock University, 1 Morrow Way, Slippery Rock, PA 16057 and Donald C. Zapien, donald.zapien@sru.edu, Department of Chemistry, Slippery Rock University, Slippery Rock, PA 16057.
In this work, the electrochemical properties of horse spleen ferritin covalently immobilized on gold are investigated. Immobilization in this fashion allows study under a wide set of solution conditions while the protein suffers minimal detachment from the surface. Adsorbed layers of carboxylic acid-terminated alkanethiols were used to modify gold surfaces. A zero-length carbodiimide linkage was made between the adsorbed layer and natural horse spleen ferritin. Cyclic voltammetry shows that the tethered ferritin is electroactive. The electrochemical characterization includes investigation of the peak area dependence on adsorbed layer chain length and ionic strength, the peak current dependence on scan rate, and a study comparing the voltammetry of natural ferritin with that of apoferritin and reconstituted ferritin.
 

General Posters
7:00 PM-9:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Analytical Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007