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Genetically synthesized antibody-binding protein self-assembled on hydrophobic matrix

Authors
Sugihara, TsutomuSeong, Gi HunKobatake, EiryAizawa, 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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COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles

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ERICA 첨단융합대학 (ERICA 바이오나노공학전공)
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