The addition of the protein, cytochrome c (cyt. c), to gold nanoparticles in solution results in self-organization of cyt. c into multilayered protein superstructures (abbreviated as Au~cyt. c superstructures) and stabilizes the thousands of organized cyt. c proteins to unfolding both when encapsulated in porous solids and when remaining in solution. Our research has shown that the electrochemical characteristics of superstructure-assembled cyt. c are enhanced compared to cyt. c alone and vary as the ratio of cyt. c to Au varies and as the size of the Au nanoparticle varies. In order to determine whether the enhanced electrochemical properties are directly related to multiple protein layers of certain types of superstructures staying intact at the electrode surface, protein superstructures made from 5-nm gold nanoparticles were stripped from electrode surfaces, measured with UV-visible spectroscopy, and compared to superstructures made from 10-nm gold nanoparticles. The UV-visible absorbance of the cyt. c Soret peak, and subsequent calculated cyt. c electrode surface coverages will be presented to help narrow in further on the cause of the enhanced electrochemical properties of certain types of superstructure-assembled cyt. c proteins. These results may prove useful to those developing bioanalytical devices when a good understanding of the interaction between protein and material surface is needed.

Complementing electrochemical studies of self-organized gold nanoparticle~cytochrome c superstructures with UV-visible spectroscopy

252nd National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.