Molecular docking and molecular dynamics studies reveal structural basis of inhibition and selectivity of inhibitors EGCG and OSU-03012 toward glucose regulated protein-78 (GRP78) overexpressed in glioblastoma

Journal of Molecular Modeling

Volumn 21, Issue 10, 2015, Pages

  Bhattacharjee, Rituparna ^a   Devi, Arpita ^a   Mishra, Seema ^a  

^a UNIVERSITY OF HYDERABAD   (India)

Author keywords

EGCG; Glioblastoma; Glucose regulated protein 78 (GRP78); Heat shock protein 70; MM PBSA; Molecular docking; Molecular dynamics; OSU 03012; Selectivity; Unfolded protein response (UPR)

Indexed keywords

2 AMINO N [4 [5 (2 PHENANTHRENYL) 3 TRIFLUOROMETHYL 1H PYRAZOL 1 YL]PHENYL]ACETAMIDE; AMINO ACID; EPIGALLOCATECHIN GALLATE; GLUCOSE REGULATED PROTEIN 78; CATECHIN; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; PROTEIN BINDING; PYRAZOLE DERIVATIVE; SULFONAMIDE;

ALPHA HELIX; ARTICLE; BETA SHEET; BINDING AFFINITY; BINDING SITE; CARCINOGENESIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; DRUG BINDING; DRUG SELECTIVITY; DRUG STABILITY; DRUG STRUCTURE; GLIOBLASTOMA; HUMAN; HUMAN CELL; HYDROGEN BOND; HYDROLYSIS; LIGAND BINDING; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; STATIC ELECTRICITY; UNFOLDED PROTEIN RESPONSE; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; GENE EXPRESSION; GENETICS; METABOLISM; MOLECULAR GENETICS; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CATECHIN; GENE EXPRESSION; GLIOBLASTOMA; HEAT-SHOCK PROTEINS; HUMANS; HYDROGEN BONDING; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PYRAZOLES; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; SEQUENCE ALIGNMENT; SULFONAMIDES;

EID: 84942803714     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-015-2801-3     Document Type: Article

References (28)

1. Goodenberger ML, Jenkins RB et al. (2012) Genetics of adult glioma. Cancer Genet 205(12):613–621
2. Ostrum QT, Bauchet L, Davis FG et al. (2014) The epidemiology of glioma in adults: a “state of the science” review. Neuro Oncol 16(7):896–913
3. Schwartzbaum JA, Fisher JL, Aldape KD et al (2006) Epidemiology and molecular pathology of glioma. Nat Clin Pract Neurol 2:493–503
4. Wang P, Dang Q, Zhang C et al (2013) Mutations in isocitrate dehydrogenase 1 and 2 occur frequently in intrahepatic cholangiocarcinomas and share hypermethylation targets with glioblastomas. Oncogene 32:3000–3091
5. Mishra S (2014) CSNK1A1 and Gli2 as novel targets identified through an integrative analysis of gene expression data, protein-protein interaction and pathways networks in glioblastoma tumors: can these two be antagonistic proteins? Cancer Informat 13:93–108
6. Pyrko P, Schönthall AH, Hofman FM et al (2007) The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas. Cancer Res 67:9809–9816
7. Li J, Lee AS (2006) Induction of GRP78/BiP and its role in cancer. Curr Mol Med 6:45–54
8. Lee AS (2007) GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res 67(8):3496–3499
9. Booth L, Cazanave SC, Hamid HA et al (2012) OSU-03012 suppresses GRP78/BiP expression that causes PERK-dependent increases in tumor cell killing. Cancer Biol Ther 13(4):224–236
10. Mayer M, Kies U, Kammermeier R et al (2000) BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 275(38):29421–29425
11. Lee HK, Xiang C, Cazacu S et al (2008) GRP78 is overexpressed in glioblastomas and regulates glioma cell growth and apoptosis. Neurooncology 10:236–243
12. Huber-Keener KJ, Yang J-M (2011) Impact of metabolic and therapeutic stresses on glioma progression and therapy. In: Chen CC (ed) Advances in the biology, imaging and therapies for glioblastoma. InTech, Rijeka, pp 23–52
13. Macias AT, Williamson DS, Allen N et al (2011) Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity. J Med Chem 54(12):4034–4041
14. Lee JY, Jung KW, Kim Y (2008) Inhibitor design for human heat shock protein 70 ATPase domain by pharmacophore-based in silicoscreening. Bull Korean Chem Soc 29(9):1717–1722
15. Ermakova SP, Kang SB, Choi BY et al (2006) (−)-Epigallocatechingallate overcomes resistance to etoposide-induced cell death by targeting the molecular chaperone glucose-regulated protein 78. Cancer Res 66(18):9260–9269
16. Martin S, Lamb HK, Brady C et al (2013) Inducing apoptosis of cancer cells using small-molecule plant compounds that bind to GRP78. Br J Cancer 109:433–443
17. Yokoyama S, Hirano H, Wakimaru N et al (2001) Inhibitory effect of epigallocatechin-gallate on brain tumor cell lines in vitro. Neuro-Oncology 3:22–28
18. Porchia LM, Guerra M, Yang YC et al (2007) 2-Amino-N-{4-[5-(2-phenanthrenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]-phenyl} acetamide (OSU-03012), a celecoxib derivative, directly targets p21-activated kinase. Mol Pharmacol 72:1124–1131
19. Booth L, Roberts JL, Tavallai M et al (2015) OSU-03012 and Viagra treatment inhibits the activity of multiple chaperone proteins and disrupts the blood brain barrier: implications for anti-cancer therapies. J Cell Physiol. doi:10.1002/jcp.24977
20. Smith TJ (2011) Green Tea Polyphenols in drug discovery — a success or failure? Expert Opin Drug Discov 6:589–595
21. Trott O, Olson AJ (2010) AutoDockVina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J Comput Chem 31(2):455–461
22. Lyskov S, Chou FC, Conchúir SÓ, Der BS, Drew K, Kuroda D, Xu J, Weitzner BD, Renfrew PD, Sripakdeevong P, Borgo B, Havranek JJ, Kuhlman B, Kortemme T, Bonneau R, Gray JJ, Das R (2013) Serverification of molecular modeling applications: The Rosetta Online Server That Includes Everyone (ROSIE). PLoS One 8(5), e63906
23. Pronk S, Pall S, Schulz R et al (2013) GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29:845–854
24. Kumari R, Kumar R, Open Source Drug Discovery Consortium, Lynn A (2014) g_mmpbsa—A GROMACS tool for high-throughput MM-PBSA calculations. J Chem Inf Model 54(7):1951–1962
25. Humphrey W, Dalke A, Schulten K (1996) VMD — visual molecular dynamics. J Mol Graph 14:33–38
26. Wisniewska M, Karlberg T, Lehtiö L, Johansson I, Kotenyova T et al (2010) Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B’, and HSPA5/BiP/GRP78. PLoS One 5(1), e8625
27. Jones NA, Spina D, Page CP (2003) Theophylline and selective phosphodiesterase inhibitors. In: Spina D, Page CP, Metzger WJ, O’Connor BJ (eds) Drugs for the treatment of respiratory diseases. Cambridge University Press, Cambridge, pp 136–171
28. Chiosis G, Timaul MN, Lucas B, Munster PN, Zheng FF, Sepp-Lorenzino L, Rosen N (2001) A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem Biol 8(3):289–299