Abstract
Abstract Previously, we constructed nickel-coated glass slides to immobilize histidine-tagged proteins [Bull. Korean Chem. Soc. 23 (2002) 1724–1728]. Here, we further investigated whether the nickel-coated glass slide could be utilized for assaying molecular interaction between lipid and immobilized protein. Proteins interact with various lipid molecules in biological systems. More importantly, this interaction is responsible for a broad spectrum of physiological functions. Accordingly, to more efficiently analyze various types of interactions and understand the complicated biological systems, it is essential to develop a high-throughput analytical device. For the high-throughput analytical purpose, we immobilized an FITC (fluorescein isothiocyanate)-tagged lipid-binding protein to nickel-coated plates, incubated the plates with various lipid molecules and then measured fluorescence intensities to analyze its binding affinity. Our systems seemed to be reliable for the application to the high-throughput system consisted of lipid-binding proteins.
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