Combining QCM and SERS on a Nanophotonic Chip: A Dual-Functional Sensor for Biomolecular Interaction Analysis and Protein Fingerprinting.
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| Title: | Combining QCM and SERS on a Nanophotonic Chip: A Dual-Functional Sensor for Biomolecular Interaction Analysis and Protein Fingerprinting. |
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| Authors: | Bartolini, Cosimo1,2 (AUTHOR), Tozzetti, Martina1,2 (AUTHOR), Gellini, Cristina1 (AUTHOR), Ricci, Marilena1,2 (AUTHOR), Menichetti, Stefano1 (AUTHOR), Procacci, Piero1 (AUTHOR), Caminati, Gabriella1,2 (AUTHOR) gabriella.caminati@unifi.it |
| Source: | Nanomaterials (2079-4991). Aug2025, Vol. 15 Issue 16, p1230. 24p. |
| Subjects: | Biosensors, Quartz crystal microbalances, Molecular recognition, Nanophotonics, Intermolecular interactions, SERS spectroscopy, Peptide mass fingerprinting |
| Abstract: | We present a dual biosensing strategy integrating Quartz Crystal Microbalance (QCM) and Surface-Enhanced Raman Spectroscopy (SERS) for the quantitative and molecular-specific detection of FKBP12. Silver nanodendritic arrays were electrodeposited onto QCM sensors, optimized for SERS enhancement using Rhodamine 6G, and functionalized with a custom-designed receptor to selectively capture FKBP12. QCM measurements revealed a two-step Langmuir adsorption behavior, enabling sensitive mass quantification with a low limit of detection. Concurrently, in situ SERS analysis on the same sensor provided vibrational fingerprints of FKBP12, resolved through comparative studies of the free protein, surface-bound receptor, and surface-bound receptor–protein complex. Ethanol-induced denaturation confirmed protein-specific peaks, while shifts in receptor vibrational modes—linked to FKBP12 binding—demonstrated dynamic molecular interactions. A ratiometric parameter, derived from key peak intensities, served as a robust, concentration-dependent signature of complex formation. This platform bridges quantitative (QCM) and structural (SERS) biosensing, offering real-time mass tracking and conformational insights. The nanodendritic substrate's dual functionality, combined with the receptor's selectivity, advances label-free protein detection for applications in drug diagnostics, with potential adaptability to other target analytes. [ABSTRACT FROM AUTHOR] |
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| Database: | Engineering Source |
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