2006年
Surface modification of thin polyion complex film with a high specific binding affinity and prevention of non-specific adsorption in surface plasmon resonance immunoassay
Electrochemistry
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 74
- 号
- 2
- 開始ページ
- 121
- 終了ページ
- 124
- DOI
- 10.5796/electrochemistry.74.121
The non-labeled and direct immunoassay of cytokine on a thin polyion complex film of poly-L-lysine and poly-styrenesulfonate was studied using a surface plasmon resonance sensor. The suppression of non-specific protein adsorption was investigated by changing the blend ratio of poly-L-lysine and poly-styrenesulfonate. With our film, the protein adsorption fell to less than 10% of that of an unmodified surface when the poly-L-lysine to poly-styrenesulfonate ratio was 4:6. We also measured the kinetic rates between tumor necrosis factor-α and anti-tumor necrosis factor-α antibodies, which were immobilized on the film. The binding constant was calculated to be 1.5×108 (M-1), which satisfies the binding constant level for a monoclonal antibody modified on a commercially available surface.
- リンク情報
- ID情報
-
- DOI : 10.5796/electrochemistry.74.121
- ISSN : 1344-3542
- identifiers.cinii_nr_id : 9000239248799
- SCOPUS ID : 33645294404