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<p>Surface Plasmon Resonance (SPR) is a highly sensitive, label-free optical technique that enables real-time monitoring of biomolecular interactions by detecting refractive index changes at a metal-dielectric interface. Owing to its high sensitivity, low sample consumption, and compatibility with high-throughput analysis, SPR has emerged as a powerful platform in biomedical research and drug discovery. It facilitates direct analysis of interactions between immobilized ligands and analytes, including protein-protein, protein-peptide, protein-nucleic acid, protein-carbohydrate, lipid-protein, and small molecule interactions, as well as those involving non-biological surfaces. By providing both kinetic (association and dissociation rates) and affinity parameters, SPR offers critical insights into the mechanistic basis of molecular recognition and signaling processes. These capabilities make it an vital tool for understanding ligand-receptor interactions, which are central to cellular signaling and therapeutic targeting, thereby supporting rational drug design and translational research. This review presents a comprehensive overview of SPR based biomolecular interaction analysis, highlighting its applications in antigen-antibody binding, epitope mapping, protein-protein interactions, and inhibitor screening. It further emphasizes the integration of kinetic modeling, mass transport considerations, and advanced analytical frameworks to improve data interpretation. In addition, recent technological advancements, key challenges, and emerging opportunities are critically discussed, underscoring the expanding role of SPR biosensors in molecular detection across diverse scientific disciplines.</p> Graphical Abstract <p></p>

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Surface plasmon resonance in drug discovery: advances in protein-protein interaction and its kinetic analysis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月17日

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  • Diwakar Kumar Singh,
  • Sameer Tiwari,
  • Kumari Kripalata

摘要

Surface Plasmon Resonance (SPR) is a highly sensitive, label-free optical technique that enables real-time monitoring of biomolecular interactions by detecting refractive index changes at a metal-dielectric interface. Owing to its high sensitivity, low sample consumption, and compatibility with high-throughput analysis, SPR has emerged as a powerful platform in biomedical research and drug discovery. It facilitates direct analysis of interactions between immobilized ligands and analytes, including protein-protein, protein-peptide, protein-nucleic acid, protein-carbohydrate, lipid-protein, and small molecule interactions, as well as those involving non-biological surfaces. By providing both kinetic (association and dissociation rates) and affinity parameters, SPR offers critical insights into the mechanistic basis of molecular recognition and signaling processes. These capabilities make it an vital tool for understanding ligand-receptor interactions, which are central to cellular signaling and therapeutic targeting, thereby supporting rational drug design and translational research. This review presents a comprehensive overview of SPR based biomolecular interaction analysis, highlighting its applications in antigen-antibody binding, epitope mapping, protein-protein interactions, and inhibitor screening. It further emphasizes the integration of kinetic modeling, mass transport considerations, and advanced analytical frameworks to improve data interpretation. In addition, recent technological advancements, key challenges, and emerging opportunities are critically discussed, underscoring the expanding role of SPR biosensors in molecular detection across diverse scientific disciplines.

Graphical Abstract