The relentless research in material science is pushing towards sustainable building blocks, which may be exploited in the molecularly imprinting technology, a potentially ground-breaking tool for producing affinity mimetic receptors. In this scenario, we report and characterize a novel polynorepinephrine (PNE)-based mimetic for IgG detection, biomolecules of utmost clinical interest, coupled to a label-free and real-time sensing based on Surface Plasmon Resonance (SPR). A "molecular walk" around the Y-shaped IgG structure is performed to select small peptide portions to be used as templates during the epitope imprinting process. For real-time diagnosis, the mimetic receptor is integrated into SPR sensing platform, to directly target the IgG both in standard solutions and human serum specimens using the standard addition method. The designed platform is characterized in terms of binding kinetic/affinity parameters and analytical figures of merit, (selectivity, repeatability, limit of detection and quantification, namely 0.90 ± 0.02 μg mL-1 and 3.01 ± 0.07 μg mL-1, respectively), displaying excellent promising outcomes also when the material is subjected to thermal stress. Comprehensively, the excellent analytical performances of the MIP-based SPR sensing and the well-known versatility of such biopolymer encourage the further development of serological point-of-care testing for IgG antibodies detection.
Imprinted biopolymers as green abiotic route in immunoglobulin affinity plasmonic sensing
Battaglia, Federica;Minunni, Maria
2022-01-01
Abstract
The relentless research in material science is pushing towards sustainable building blocks, which may be exploited in the molecularly imprinting technology, a potentially ground-breaking tool for producing affinity mimetic receptors. In this scenario, we report and characterize a novel polynorepinephrine (PNE)-based mimetic for IgG detection, biomolecules of utmost clinical interest, coupled to a label-free and real-time sensing based on Surface Plasmon Resonance (SPR). A "molecular walk" around the Y-shaped IgG structure is performed to select small peptide portions to be used as templates during the epitope imprinting process. For real-time diagnosis, the mimetic receptor is integrated into SPR sensing platform, to directly target the IgG both in standard solutions and human serum specimens using the standard addition method. The designed platform is characterized in terms of binding kinetic/affinity parameters and analytical figures of merit, (selectivity, repeatability, limit of detection and quantification, namely 0.90 ± 0.02 μg mL-1 and 3.01 ± 0.07 μg mL-1, respectively), displaying excellent promising outcomes also when the material is subjected to thermal stress. Comprehensively, the excellent analytical performances of the MIP-based SPR sensing and the well-known versatility of such biopolymer encourage the further development of serological point-of-care testing for IgG antibodies detection.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.