Enhancement of BSA Binding on Au Surfaces by calix[4]bisazacrown Monolayer

Effective investigation of biomolecular structure and function with chip-basedmodern instruments often requires reliable and steady attachment of designatedbiomolecules on substrate. Here, we investigated the formation of self-assembled monolayer(SAM) with a new calix[4]arene derivative containing bisazacrown ether at the lower rim(calix[4]bisazacrown) where ammonium moieties of proteins can mainly be interacted with.Immobilization process of protein using bovine serum albumin (BSA) on the Au surfacemodified with calix[4]bisazacrown monolyer as an artificial linker system was monitored bysurface plasmon resonance (SPR) technique. The surface concentration of BSA calculatedby the simulation of SPR experimental data was higher than that of a well-known similarcommercial protein linker. These results can help in modeling and understanding of proteinimmobilization on solid surface as well as further development lab-on-a-chip (LOC) devicesfor biomedical diagnosis kit of certain protein related diseases as biomarkers.