Earticle

초록

영어

Surface modification and optimization is a principal part in developing a high sensitivity and high capacity protein sensor as an advanced immunoassay. To increase and improve the binding density of biomolecules on the surface matrices with biomolecules, dendrimer generation 4.5, which was terminated with carboxyl group (PAMAM-COOH), was layered on amine functionalized glass by covalent bonding. The surface properties were analyzed by ellipsometer and scanning electron microscopy to optimize the dispersion of the polymer and the chemistry for immobilization of proteins. IgG whole molecules (H+L) and Fc cleaved antibodies containing variable region were tested as protein-binding agents on the dendrimers and unbound free amines on the surfaces were capped by BSA or small PEG derivatives.
This study demonstrates high-sensitivity by following attachment of covalent bond formation as compared with blank glass supports. Moreover, dendrimer-driven increased binding capacity was demonstrated with fragmented antibodies by reducing steric hindrance/resistance among the polymer and biomolecules and by inhibiting non-specific binding and undesired direct coupling between carboxylic acids of Antibody heavy chains and amines on the glass surfaces.

저자

• Jung-Sun Lim [ Battelle@KU, Battelle-Korea, Techno Complex Research Center, Korea University ]
• Chang-Woo Lee [ Battelle@KU, Battelle-Korea, Techno Complex Research Center, Korea University ]
• Hyo-Sun Kim [ Battelle@KU, Battelle-Korea, Techno Complex Research Center, Korea University ]
• Yang-Eon Kim [ Battelle@KU, Battelle-Korea, Techno Complex Research Center, Korea University ]
• Victor S. Moore [ Battelle@KU, Battelle-Korea, Techno Complex Research Center, Korea University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576