Genetically synthesized antibody-binding protein self-assembled on hydrophobic matrix
- Authors
- Sugihara, Tsutomu; Seong, Gi Hun; Kobatake, Eiry; Aizawa, Masuo
- Issue Date
- Nov-2000
- Publisher
- AMER CHEMICAL SOC
- Citation
- BIOCONJUGATE CHEMISTRY, v.11, no.6, pp 789 - 794
- Pages
- 6
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCONJUGATE CHEMISTRY
- Volume
- 11
- Number
- 6
- Start Page
- 789
- End Page
- 794
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/46942
- DOI
- 10.1021/bc000031j
- ISSN
- 1043-1802
1520-4812
- Abstract
- A unique antibody-binding protein, (E12B2)n, was genetically synthesized, which was characterized by a hydrophobic peptide, E12, at one terminus and an antibody-binding peptide, B2, at the other. It was clarified by atomic force microscopy (AFM) imaging that this protein was efficiently self-assembled on a hydrophobic solid surface. (E12B2)n self-assembled on a microplate exhibited an excellent performance of antibody-binding affinity. The proposed design of antibody-binding protein seems promising in immobilizing antibody molecules on hydrophobic solid surfaces.
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Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles

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