6533b834fe1ef96bd129d58a

RESEARCH PRODUCT

Experimental Study of the Oriented Immobilization of Antibodies on Photonic Sensing Structures by Using Protein A as an Intermediate Layer

Jorge EscorihuelaMaría-josé BañulsRaffaele CaroselliÁNgel MaquieiraJ. G. CastellóJaime García-rupérez

subject

AnalyteMaterials scienceIntegrated photonicsSerum albuminBiosensing TechniquesRing resonator02 engineering and technologylcsh:Chemical technologyBiotecnologia01 natural sciencesBiochemistryAntibodiesArticleAnalytical Chemistry010309 opticsResonatorring resonatorsensorQUIMICA ANALITICATEORIA DE LA SEÑAL Y COMUNICACIONES0103 physical scienceslcsh:TP1-1185Electrical and Electronic EngineeringStaphylococcal Protein AInstrumentationIntegrated photonics; ring resonator; sensor; biosensingSensorDetection limitPhotonsChromatographybiologyBiosensingbusiness.industrySerum Albumin BovineRepeatabilityÒptica021001 nanoscience & nanotechnologyAtomic and Molecular Physics and Opticsbiology.proteinbiosensingPhotonics0210 nano-technologybusinessProtein ABiosensor

description

[EN] A proper antibody immobilization on a biosensor is a crucial step in order to obtain a high sensitivity to be able to detect low target analyte concentrations. In this paper, we present an experimental study of the immobilization process of antibodies as bioreceptors on a photonic ring resonator sensor. A protein A intermediate layer was created on the sensor surface in order to obtain an oriented immobilization of the antibodies, which enhances the interaction with the target antigens to be detected. The anti-bovine serum albumin (antiBSA)-bovine serum albumin (BSA) pair was used as a model for our study. An opto-fluidic setup was developed in order to flow the different reagents and, simultaneously, to monitor in real-time the spectral response of the photonic sensing structure. The antiBSA immobilization and the BSA detection, their repeatability, and specificity were studied in different conditions of the sensor surface. Finally, an experimental limit of detection for BSA recognition of only 1 ng/mL was obtained

https://doi.org/10.3390/s18041012