Biomolecular Memory Device Composed of Cytochrome c on a Self-Assembled 11-Mercaptoundecanoic Acid Layer

Abstract

In this study, we developed an advanced molecular memory device that was based on covalently attaching cytochrome c/11-mercaptoundecanoic acid to Au surfaces. Cytochrome c has redox properties, which can be used to store information when coupled into a molecular device. Cytochrome c was immobilized onto Au substrates using the chemical linker 11-mercaptoundecanoic acid. The immobilization of cytochrome c was verified by surface plasmon resonance spectroscopy and the structure of immobilized cytochrome c was determined by scanning tunneling microscopy. In addition, the redox properties of the cytochrome c layer was verified by cyclic voltammetry. Furthermore, the two states memory characteristics of the fabricated film was demonstrated using chronoamperomemtry and the three states memory performance of the device was assessed using open circuit potential amperomemtry. Based on the combined results of this study, it could be concluded that the cytochrome c layer could be used as a nanobiochip platform for memory storage.

Fatigue Test of Cytochrome C Self-Assembled on a 11-MUA Layer Based on Electrochemical Analysis for Bioelectronic Device

“…11 Recently, a bioememory device containing cytochrome c or recombinant azurin has been developed by introducing of biological functions into a conventional silicon-based electronic 12 13 Various types of biomemory devices have been proposed based on the self-assembly technique. [14][15][16] However, previous studies only proposed the basic operation mechanism of the memory operating principle. For developing the biomemory device practically, it is necessary to understand the electrochemical property of the heterolayer in harsh conditions such as variation of temperature and pH, and durability (repetition of usage).…”

Cytochrome c552 from Thermus thermophilus Engineered for Facile Substitution of Prosthetic Group

“…Thus, Cyt c has been used as a major resource for basic biochemical and biophysical studies on the folding and unfolding mechanisms of proteins, − intramolecular electron transfer mechanisms, , and specific interprotein interaction mechanisms. , In addition to these fundamental studies, the application of Cyt c in biomaterials research has emerged as a current topic. For example, oxidase activity introduced to Cyt c has been studied in the construction of artificial heme enzymes. ,− Methods for the modification of an electrode with Cyt c by various methods has also been developed to apply the protein to bioelectronic devices such as biomemory devices, − biodiodes, and biofuel cells and for use in bio-photoswitching functions. ,, The thioether bonds located between the polypeptide and the heme moiety in Cyt c contribute to improve stability of the biomaterials produced . However, further development and evolution of the Cyt c -based materials are limited due to the stable covalent linkages and the difficulty in replacing the heme c with an artificial prosthetic group having non-natural function­(s). , In order to overcome the limitations, engineered Cyt c should (i) contain a readily removable heme species, (ii) be capable of incorporating non-natural prosthetic groups through reconstitution, and (iii) have the ability to form covalent linkage­(s) with the reconstituted external prosthetic group.…”