An Optofluidic Guided-Mode Resonance Platform for Binding Kinetics Applications
IEEE SENSORS JOURNAL, vol.25, no.3, pp.4481-4493, 2025 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 25 Issue: 3
- Publication Date: 2025
- Doi Number: 10.1109/jsen.2024.3515653
- Journal Name: IEEE SENSORS JOURNAL
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aerospace Database, Communication Abstracts, Compendex, INSPEC, Metadex, Civil Engineering Abstracts
- Page Numbers: pp.4481-4493
- Keywords: Binding dynamics, guided mode resonance (GMR), label-free biosensing, nanotechnology, optofluidic, Binding dynamics, guided mode resonance (GMR), label-free biosensing, nanotechnology, optofluidic
- Dokuz Eylül University Affiliated: No
Abstract
Guided mode resonance (GMR) sensors have emerged as transformative tools in sensing technology, offering exceptional sensitivity, selectivity, and real-time, label-free detection capabilities across diverse applications, including medical diagnostics and environmental monitoring. Their miniaturization potential, cost-effective manufacturing, and wide dynamic range make GMR sensors highly versatile and commercially attractive. In this study, we present an optofluidic GMR platform tailored for real-time analysis of biomolecular interactions without the need for optical labels. The platform integrates a custom-built inverted microscopy system, a high-resolution multispectrometer setup with a spectral resolution of 0.15 nm, and an automated multipump fluid control system, enabling precise and efficient monitoring of binding kinetics between biomolecules. Key outcomes include a refractive index sensitivity of 201.73 nm/RIU and a demonstrated detection limit of 0.15 ng/mL for IgG protein, emphasizing the platform's suitability for highly sensitive biodetection applications. Additionally, the automated flow methodology enhances efficiency and reproducibility by streamlining chip preparation, ligand/analyte incubation, and postexperiment cleaning, minimizing manual intervention and human error. The self-cleaning feature ensures contamination-free operation, facilitating seamless multiuse experiments. Furthermore, we determined the association constant during the binding of protein A/G and IgG, underscoring the platform's applicability to real-time binding kinetics studies. These results establish our optofluidic GMR platform as a robust and precise tool for advancing the understanding of complex biomolecular processes.