Surface plasmon resonance characterization of photoswitchable antigen-antibody interactions

Citation
E. Kaganer et al., Surface plasmon resonance characterization of photoswitchable antigen-antibody interactions, LANGMUIR, 15(11), 1999, pp. 3920-3923
Citations number
38
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
LANGMUIR
ISSN journal
07437463 → ACNP
Volume
15
Issue
11
Year of publication
1999
Pages
3920 - 3923
Database
ISI
SICI code
0743-7463(19990525)15:11<3920:SPRCOP>2.0.ZU;2-U
Abstract
Photostimulated association and dissociation of anti-dinitrophenyl antibody , anti-DNP-Ab, to and from a dinitrospiropyran photoisomerizable monolayer is probed by surface plasmon resonance (SPR). The anti-DNP-Ab binds to a di nitrospiropyran antigen monolayer, whereas the DNP-AI, dissociates from the protonated dinitromerocyanine monolayer. Reversible binding and dissociati on of anti-DNP-Ab to and from the photoisomerizable monolayer was assayed b y SPR spectroscopy. Analysis of the SPR data indicates that the average thi ckness of the antibody layer is ca. 70 Angstrom which corresponds to a surf ace coverage of ca. 4.4 x 10(-9) mol.cm(-2).