Nanoscale Biofilm Modification-Method Concerning a Myoglobin/11-MUA Bilayers for Bioelectronic Device

  • Lee, Taek; 
  • Chung, Yong-Ho; 
  • Chen, Qi; 
  • El-Said, Waleed Ahmed; 
  • Min, Junhong; 
  • 외 1명
Citations

WEB OF SCIENCE

5
Citations

SCOPUS

6

초록

We developed surface modification tools for the fabrication of a bioelectronic device which consists of a myoglobin monolayer self-assembled on an 11-MUA layer. To utilize a single protein as the active element, it was necessary to reduce protein aggregation on the protein layer in the nanobio electronic device, which was developed in our previous study and shown to display basic biomemory functions. Here, the reduction of myoglobin aggregation was accomplished by using 3-(3-cholamidopropyl) dimethylammonio-1-propanesulfonate (CHAPS) to fabricate a well-defined protein layer on the bioelectronic device. We investigated two different surface modification methods for making well oriented biofilm. The effects of CHAPS on the formation of a myoglobin layer self-assembled on an 11-MUA layer were examined by atomic force microscopy and Raman spectroscopy. The size of the myoglobin aggregates was reduced from 200 similar to 250 nm to 10 similar to 40 nm depending on treatment method. The sustaining redox property of the CHAPS treated myoglobin layer was examined using cyclic voltammetry. Using these techniques, we found that after surfactant CHAPS treatment, protein aggregation was dramatically reduced and the protein layer still maintained its inherent electrochemical properties.

키워드

Myoglobin; Bioelectronic Device; CHAPS; Atomic Force Microscopy; Cyclic Voltammetry; NONVOLATILE MEMORY; BIOMEMORY DEVICE; MONOLAYER; PHOTODIODE; RAMAN
제목
Nanoscale Biofilm Modification-Method Concerning a Myoglobin/11-MUA Bilayers for Bioelectronic Device
저자
Lee, Taek; Chung, Yong-Ho; Chen, Qi; El-Said, Waleed Ahmed; Min, Junhong; Choi, Jeong-Woo
DOI
10.1166/jnn.2012.5904
발행일
2012-05
유형
Article; Proceedings Paper
저널명
Journal of Nanoscience and Nanotechnology
권
12
호
5
페이지
4119 ~ 4126