Jafar Ezzati Nazhad Dolatabadi
1*, Miguel De la Guardia
21 Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran
2 Department of Analytical Chemistry, University of Valencia, Valencia, Spain
Abstract
Surface plasmon resonance (SPR) technique offers a robust label-free approach applicable in various investigations including binding affinity, specificity and kinetics of biological macromolecules (e.g., peptides, proteins and nucleotidase) and small molecules. SPR provides extremely important data on the kinetics and affinity of substances examined, through which bio-specific interaction(s) can be established by the analysis of adsorption of analyte onto the immobilized ligand(s) on a sensor-based analytical system. Due to SPR wide applications in biomedical laboratories, the aim of this editorial is to highlight the importance of SPR in affinity kinetics and ligand immobilization.