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

被引:23
作者
Ghosh, Srabanti [1 ]
Ray, Manju [2 ]
Das, Mahua Rani [3 ]
Chakrabarti, Adrita [1 ]
Khan, Ali Hossain [1 ]
Sarma, D. D. [4 ,5 ]
Acharya, Somobrata [1 ]
机构
[1] Indian Assoc Cultivat Sci, Ctr Adv Mat, Kolkata 700032, India
[2] Bose Inst, Div Mol Med, Kolkata 700054, India
[3] Indian Assoc Cultivat Sci, Kolkata 700032, India
[4] Indian Inst Sci, Solid State & Struct Chem Unit, Bangalore 560012, Karnataka, India
[5] Indian Inst Sci, Ctr Condensed Matter Theory, Bangalore 560012, Karnataka, India
关键词
MALIGNANT-CELLS; COMPLEX I; INHIBITION; PROTEIN; INACTIVATION;
D O I
10.1039/c3cp53489h
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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.
引用
收藏
页码:5276 / 5283
页数:8
相关论文
共 50 条
[41]   Sevoflurane modulates the activity of glyceraldehyde 3-phosphate dehydrogenase [J].
Swearengin, Timothy A. ;
Fibuch, Eugene E. ;
Seidler, Norbert W. .
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2006, 21 (05) :575-579
[42]   Products of S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase: Relation between S-nitrosylation and oxidation [J].
Schmalhausen, E., V ;
Medvedeva, M., V ;
Serebryakova, M., V ;
Chagovets, V. V. ;
Muronetz, V., I .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2022, 1866 (01)
[43]   Structural Insights into RNA Recognition Properties of Glyceraldehyde-3-phosphate Dehydrogenase 3 from Saccharomyces cerevisiae [J].
Shen, Hui ;
Wang, Hong ;
Liu, Qiao ;
Liu, Huihui ;
Teng, Maikun ;
Li, Xu .
IUBMB LIFE, 2014, 66 (09) :631-638
[44]   Glyceraldehyde-3-phosphate dehydrogenase present in extracellular vesicles from Leishmania major suppresses host [J].
Das, Priya ;
Mukherjee, Aditi ;
Adak, Subrata .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2021, 297 (04)
[45]   Phosphatidic Acid Binds to Cytosolic Glyceraldehyde-3-phosphate Dehydrogenase and Promotes Its Cleavage in Arabidopsis [J].
Kim, Sang-Chul ;
Guo, Liang ;
Wang, Xuemin .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (17) :11834-11844
[46]   Biochemical characterization of glyceraldehyde-3-phosphate dehydrogenase from Thermococcus kodakarensis KOD1 [J].
Jia, Baolei ;
Le Thuy Linh ;
Lee, Sangmin ;
Bang Phuong Pham ;
Liu, Jinliang ;
Pan, Hongyu ;
Zhang, Shihong ;
Cheong, Gang-Won .
EXTREMOPHILES, 2011, 15 (03) :337-346
[47]   Effects of the Cobalt-60 gamma radiation on Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase [J].
Iddar, Abdelghani ;
El Mzibri, Mohammed ;
Moutaouakkil, Adnane .
INTERNATIONAL JOURNAL OF RADIATION BIOLOGY, 2022, 98 (02) :244-252
[48]   Pleiotropic effects of moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in cancer progression, invasiveness, and metastases [J].
Sirover, Michael A. .
CANCER AND METASTASIS REVIEWS, 2018, 37 (04) :665-676
[49]   The uncommon function and mechanism of the common enzyme glyceraldehyde-3-phosphate dehydrogenase in the metamorphosis of Helicoverpa armigera [J].
Zhao, Wenli ;
Zhang, Bo ;
Geng, Zichen ;
Chang, Yanpeng ;
Wei, Jizhen ;
An, Shiheng .
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY, 2022, 10
[50]   Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis [J].
Muronetz, Vladimir I. ;
Medvedeva, Maria V. ;
Sevostyanova, Irina A. ;
Schmalhausen, Elena V. .
BIOMOLECULES, 2021, 11 (11)