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| Main Authors: | , , , , , , , , , |
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| Format: | Preprint |
| Published: |
2024
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| Subjects: | |
| Online Access: | https://arxiv.org/abs/2401.11801 |
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| _version_ | 1866909078994812928 |
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| author | Macchia, Eleonora Di Franco, Cinzia Scandurra, Cecilia Sarcina, Lucia Piscitelli, Matteo Catacchio, Michele Caputo, Mariapia Bollella, Paolo Scamarcio, Gaetano Torsi, Luisa |
| author_facet | Macchia, Eleonora Di Franco, Cinzia Scandurra, Cecilia Sarcina, Lucia Piscitelli, Matteo Catacchio, Michele Caputo, Mariapia Bollella, Paolo Scamarcio, Gaetano Torsi, Luisa |
| contents | While nucleic-acids can be readily amplified for single-marker detection, a comparable method for proteins assay is currently unavailable. Proteins potentiometric detections at 10-20 molar have been demonstrated, but the mechanism remains elusive. Here, we unveil how pH-conditioning within the trillions of recognition elements densely packed on a millimeter-large surface, enables single protein or DNA selective detections in 0.1 mL of a biofluid. Plasmonic, electronic and surface probing techniques demonstrate that a conformational change, elicited by a single-affinity binding, alters the secondary and tertiary structure of the recognition elements. A phenomenological mechanism foresees that the pH-conditioning initiates a hydrophobization process leading to the formation of a partially aggregated and metastable state that facilitates the amplification spreading. Impact on protein aggregates control and biomarker-based diagnostics, is envisaged. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2401_11801 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | pH-conditioning of recognition layers enables single-molecule affinity detections at 10E-20 molar Macchia, Eleonora Di Franco, Cinzia Scandurra, Cecilia Sarcina, Lucia Piscitelli, Matteo Catacchio, Michele Caputo, Mariapia Bollella, Paolo Scamarcio, Gaetano Torsi, Luisa Applied Physics While nucleic-acids can be readily amplified for single-marker detection, a comparable method for proteins assay is currently unavailable. Proteins potentiometric detections at 10-20 molar have been demonstrated, but the mechanism remains elusive. Here, we unveil how pH-conditioning within the trillions of recognition elements densely packed on a millimeter-large surface, enables single protein or DNA selective detections in 0.1 mL of a biofluid. Plasmonic, electronic and surface probing techniques demonstrate that a conformational change, elicited by a single-affinity binding, alters the secondary and tertiary structure of the recognition elements. A phenomenological mechanism foresees that the pH-conditioning initiates a hydrophobization process leading to the formation of a partially aggregated and metastable state that facilitates the amplification spreading. Impact on protein aggregates control and biomarker-based diagnostics, is envisaged. |
| title | pH-conditioning of recognition layers enables single-molecule affinity detections at 10E-20 molar |
| topic | Applied Physics |
| url | https://arxiv.org/abs/2401.11801 |