Abstract
An attempt of surface modification with receptor layers to achieve a maximal signal from antigen-antibody interaction on the solid surface has been undertaken. Interaction of C-reactive protein (CRP) with monoclonal anti-CRP has been investigated by comparative study by chemical cross-linking or electrostatic interaction in the framework of Layer-by-Layer approach. The processes of gold surface modification have been monitored by a wavelength interrogation-based surface plasmon resonance (SPR) sensor. Atomic force microscopy has been used for visualization of the surfaces modified with protein layers. The influence of biotinylated protein G-streptavidin (bPG/STV) complex on the SPR signal shift by antigen-antibody interaction has been studied. The influence of different cross-linking chemicals, such as di(N-succinimidyl)-3,3′-dithiodipropionate, 3-(2-pyridyldithio)-propionic acid N-hydroxysuccinimide ester, and N-hydroxysuccinimide/N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide on antigen immobilization of anti-CRP/bPG/STV system has been also examined. The film morphology of the first immobilized layer is very important for protein interactions. Maximum SPR-shift by CRP coupling with anti-CRP has been observed on the surface modified by streptavidin and di(N-succinimidyl)-3,3′-dithiodipropionate. AFM method can be used to directly monitor CRP/anti-CRP interaction on polyelectrolyte support.
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Zhavnerko, G.K., Yi, S.J., Chung, S.H., Yuk, J.S., Ha, K.S. (2004). Oriented Immobilization of C-Reactive Protein on Solid Surface for Biosensor Applications. In: Buzaneva, E., Scharff, P. (eds) Frontiers of Multifunctional Integrated Nanosystems. NATO Science Series II: Mathematics, Physics and Chemistry, vol 152. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2173-9_10
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DOI: https://doi.org/10.1007/1-4020-2173-9_10
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