Ali, M A and Srivastava, S and Pandey, M K and Agrawal, V V and John, R and Malhotra, B D
(2014)
Protein-conjugated quantum dots interface: Binding kinetics and label-free lipid detection.
Analytical Chemistry, 86 (3).
pp. 1710-1718.
ISSN 0003-2700
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Abstract
We propose a label-free biosensor platform to investigate the binding kinetics using antigen-antibody interaction via electrochemical and surface plasmon resonance (SPR) techniques. The l-cysteine in situ capped cadmium sulfide (CdS; size < 7 nm) quantum dots (QDs) self-assembled on gold (Au) coated glass electrode have been covalently functionalized with apolipoprotein B-100 antibodies (AAB). This protein conjugated QDs-based electrode (AAB/CysCdS/Au) has been used to detect lipid (low density lipoprotein, LDL) biomolecules. The electrochemical impedimetric response of the AAB/CysCdS/Au biosensor shows higher sensitivity (32.8 kΩ μM-1/cm 2) in the detection range, 5-120 mg/dL. Besides this, efforts have been made to investigate the kinetics of antigen-antibody interactions at the CysCdS surface. The label-free SPR response of AAB/CysCdS/Au biosensor exhibits highly specific interaction to protein (LDL) with association constant of 33.4 kM-1 s-1 indicating higher affinity toward LDL biomolecules and a dissociation constant of 0.896 ms-1. The results of these studies prove the efficacy of the CysCdS-Au platform as a high throughput compact biosensing device for investigating biomolecular interactions
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