Protein-conjugated quantum dots interface: Binding kinetics and label-free lipid detection

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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IITH Creators:
IITH CreatorsORCiD
Item Type: Article
Uncontrolled Keywords: Antigen-antibody interaction; Association constant; Biomolecular interactions; Biosensing devices; Dissociation constant; Label-free biosensor; Low density lipoproteins; Specific interaction
Subjects: Biomedical Engineering
Divisions: Department of Biomedical Engineering
Depositing User: Team Library
Date Deposited: 31 Dec 2014 10:13
Last Modified: 20 Jun 2017 11:29
URI: http://raiith.iith.ac.in/id/eprint/1285
Publisher URL: http://dox.doi.org/10.1021/ac403543g
OA policy: http://www.sherpa.ac.uk/romeo/issn/0003-2700/
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