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Modulation of glyceraldehyde-3-phosphate dehydrogenase activity by surface functionalized quantum dots

Ghosh, Srabanti and Ray, Manju and Das, MahuaRani and Chakrabarti, Adrita and Khan, Ali Hossain and Sarma, DD and Acharya, Somobrata (2014) Modulation of glyceraldehyde-3-phosphate dehydrogenase activity by surface functionalized quantum dots. In: PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 16 (11). pp. 5276-5283.

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Official URL: http://dx.doi.org/10.1039/c3cp53489h

Abstract

Enzymatic regulation is a fast and reliable diagnosis tool via identification and design of inhibitors for modulation of enzyme function. Previous reports on quantum dots (QDs)-enzyme interactions reveal a protein-surface recognition ability leading to promising applications in protein stabilization, protein delivery, bio-sensing and detection. However, the direct use of QDs to control enzyme inhibition has never been revealed to date. Here we show that a series of biocompatible surface-functionalized metal-chalcogenide QDs can be used as potent inhibitors for malignant cells through the modulation of enzyme activity, while normal cells remain unaffected. The in vitro activity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), an enzyme involved critically in the glycolysis of cancer cells, is inactivated selectively in a controlled way by the QDs at a significantly low concentration (nM). Cumulative kinetic studies delineate that the QDs undergo both reversible and irreversible inhibition mechanisms owing to the site-specific interactions, enabling control over the inhibition kinetics. These complementary loss-of-function probes may offer a novel route for rapid clinical diagnosis of malignant cells and biomedical applications.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to the ROYAL SOC CHEMISTRY, ENGLAND
Department/Centre: Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Depositing User: Id for Latest eprints
Date Deposited: 12 May 2014 11:10
Last Modified: 12 May 2014 11:10
URI: http://eprints.iisc.ac.in/id/eprint/48927

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