Surface Plasmon Resonance Immunosensor for Recombinant H1N1 Protein

Abstract

This paper describes about the surface plasmon resonance (SPR) based high affinity detection of recombinant antigen H1N1 (rH1N1HA). The modification of gold SPR chip with 4-MBA and anti-rH1N1HA were in situ characterized by SPR and electrochemical impedance spectroscopy (EIS). By using kinetic evaluation software, KD and Bmax values were calculated and found to be 0.278 pM and 84.51 mo, respectively for the interaction of rH1N1HA with immobilized anti-rH1N1HA. In addition, thermodynamic parameters such as ∆G (−49.78 kJ/mol), ∆H (98.25 kcal/mol), and ∆S (72.59 cal/mol.K) were determined first time for the interaction between anti-rH1N1HA and rH1N1HA, and these values revealed that this interaction is spontaneous, endothermic, and entropy driven one. The kinetics and thermodynamic results of this study revealed that the interaction between the immobilized anti-rH1N1HA with rH1N1HA is more effective than that of interaction of anti-rH1N1HA with the immobilized rH1N1HA. The sensing linearity observed for rH1N1HA is from 0.015 pg to 1.5 ng/ml. The present SPR-based approach may be used in the hospitals equipped with SPR for the early screening of clinical samples in a label-free, real-time manner.