C2ay25780g 3718..3723
نویسندگان
چکیده
The binding interactions between ligands and receptors play a vital role in their biological functions. In this work, a label-free indirect competitive binding assay based on surface plasmon resonance (SPR) detectionwas developed, using fatty acid–human serumalbumin (HSA) as amodel system. In the assay, a fatty acid analog was immobilized on the surface of an SPR gold chip by self-assembly, and was allowed to bind with HSA in solution. Addition of a ligand under investigation into the solution set up a competitionwith the analog for the protein, causing a reduction in the SPR signal. Due to the asymmetric structure of the ligand binding channel, HSA exhibited remarkable selectivity for the orientation of the fatty acid analog on a gold surface. When the carboxylic acid group of the analog was exposed on the sensor surface, the amount of boundHSAwas very low. However, it increased bymore than 7 fold when the alkyl chain was exposed. Dilution of the surface coverage of the fatty acid analog also enhancedHSA binding by reducing steric hindrance on the surface. Using a 1 : 4 mercaptoundecanoic acid– mercaptohexanol modified surface derivatized with octylamine, competitive binding assays for octanoic acid and perfluorooctane sulfonate with HSA were conducted. Using a derived kinetic equilibrium model, the equilibrium association constant was determined to be 4.57 10 M 1 and 2.11 10 M , respectively,which are consistentwith the valuesmeasured by other establishedmethods. The engineered sensor chip surface can be used to study the binding interactions of other chemicals with this important serum transport protein.
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