EGCG in Green Tea Induces Aggregation of HMGB1 Protein through Large Conformational Changes with Polarized Charge Redistribution

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Meng, Xuan Yu ^a,d   Li, Baoyu ^a   Liu, Shengtang ^a   Kang, Hongsuk ^b   Zhao, Lin ^a   Zhou, Ruhong ^a,b,c  

^a SOOCHOW UNIVERSITY   (China)

^b IBM T J WATSON RESEARCH CENTER   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

^d VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATECHIN; CYSTEINE; EPIGALLOCATECHIN GALLATE; HIGH MOBILITY GROUP B1 PROTEIN; PROTEIN AGGREGATE; PROTEIN BINDING; TEA;

ANALOGS AND DERIVATIVES; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DRUG EFFECTS; HUMAN; METABOLISM; MOLECULAR DYNAMICS; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; PROTEINOSIS; STATIC ELECTRICITY; TEA;

BINDING SITES; CATECHIN; CYSTEINE; HMGB1 PROTEIN; HUMANS; MOLECULAR CONFORMATION; MOLECULAR DYNAMICS SIMULATION; MOLECULAR STRUCTURE; PROTEIN AGGREGATES; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN BINDING; PROTEIN DOMAINS; PROTEIN MULTIMERIZATION; STATIC ELECTRICITY; TEA;

EID: 84959017544     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep22128     Document Type: Article

References (46)

1. Lotze, M. T. & Tracey, K. J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat Rev Immunol 5, 331-342 (2005).
2. Ohndorf, U.-M., Rould, M. A., He, Q., Pabo, C. O. & Lippard, S. J. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature 399, 708-712 (1999).
3. Wang, H. et al. HMG-1 as a Late Mediator of Endotoxin Lethality in Mice. Science 285, 248-251 (1999).
4. Yang, H. et al. Reversing established sepsis with antagonists of endogenous high-mobility group box 1. Proc. Natl. Acad. Sci. USA 101, 296-301 (2004).
5. Riegsecker, S., Wiczynski, D., Kaplan, M. J. & Ahmed, S. Potential benefits of green tea polyphenol EGCG in the prevention and treatment of vascular inflammation in rheumatoid arthritis. Life Sci. 93, 307-312 (2013).
6. Li, W. et al. A Major Ingredient of Green Tea Rescues Mice from Lethal Sepsis Partly by Inhibiting HMGB1. PLoS One 2, e1153 (2007).
7. Li, W. et al. EGCG stimulates autophagy and reduces cytoplasmic HMGB1 levels in endotoxin-stimulated macrophages. Biochem. Pharmacol. 81, 1152-1163 (2011).
8. Pae, M. & Wu, D. Immunomodulating effects of epigallocatechin-3-gallate from green tea: mechanisms and applications. Food Funct. 4, 1287-1303 (2013).
9. Chung, J. E. et al. Self-assembled micellar nanocomplexes comprising green tea catechin derivatives and protein drugs for cancer therapy. Nat Nano 9, 907-912 (2014).
10. Chen, D. et al. EGCG, green tea polyphenols and their synthetic analogs and prodrugs for human cancer prevention and treatment. Adv. Clin. Chem. 53, 155-177 (2011).
11. Jankun, J., Selman, S. H., Swiercz, R. & Skrzypczak-Jankun, E. Why drinking green tea could prevent cancer. Nature 387, 561-561 (1997).
12. Shukla, R. et al. Laminin receptor specific therapeutic gold nanoparticles (198AuNP-EGCg) show efficacy in treating prostate cancer. Proc. Natl. Acad. Sci. USA 109, 12426-12431 (2012).
13. Tang, D., Kang, R., Zeh Iii, H. J. & Lotze, M. T. High-mobility group box 1 and cancer. Biochim. Biophys. Acta 1799, 131-140 (2010).
14. Liu, P., Huang, X., Zhou, R. & Berne, B. J. Observation of a dewetting transition in the collapse of the melittin tetramer. Nature 437, 159-162 (2005).
15. Das, P., King, J. A. & Zhou, R. Aggregation of gamma-crystallins associated with human cataracts via domain swapping at the C-terminal beta-strands. Proc. Natl. Acad. Sci. USA 108, 10514-10519 (2011).
16. Kang, S. G. et al. Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine. Proc. Natl. Acad. Sci. USA 109, 15431-15436 (2012).
17. Stirnemann, G., Kang, S. G., Zhou, R. & Berne, B. J. How force unfolding differs from chemical denaturation. Proc. Natl. Acad. Sci. USA 111, 3413-3418 (2014).
18. Zhou, R. Trp-cage: folding free energy landscape in explicit water. Proc. Natl. Acad. Sci. USA 100, 13280-13285 (2003).
19. Zhou, R., Berne, B. J. & Germain, R. The free energy landscape for beta hairpin folding in explicit water. Proc. Natl. Acad. Sci. USA 98, 14931-14936 (2001).
20. Zhou, R., Huang, X., Margulis, C. J. & Berne, B. J. Hydrophobic collapse in multidomain protein folding. Science 305, 1605-1609 (2004).
21. Shen, M.-y. & Sali, A. Statistical potential for assessment and prediction of protein structures. Protein Science 15, 2507-2524 (2006).
22. Hess, B., Kutzner, C., van der Spoel, D. & Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447 (2008).
23. Oostenbrink, C., Villa, A., Mark, A. E. & Van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25, 1656-1676 (2004).
24. Liu, F.-F., Dong, X.-Y., He, L., Middelberg, A. P. J. & Sun, Y. Molecular Insight into Conformational Transition of Amyloid β-Peptide 42 Inhibited by (-)-Epigallocatechin-3-gallate Probed by Molecular Simulations. J. Phys. Chem. B 115, 11879-11887 (2011).
25. Darden, T., York, D. & Pedersen, L. Particle Mesh Ewald - an N.Log(N) Method for Ewald Sums in Large Systems. J. Chem. Phys. 98, 10089-10092 (1993).
26. Berendsen, H. J. C., Postma, J. P. M., Vangunsteren, W. F., Dinola, A. & Haak, J. R. Molecular-Dynamics with Coupling to an External Bath. J. Chem. Phys. 81, 3684-3690 (1984).
27. Hess, B., Bekker, H., Berendsen, H. J. C. & Fraaije, J. G. E. M. LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472 (1997).
28. Das, P., Kapoor, D., Halloran, K. T., Zhou, R. & Matthews, C. R. Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study. J. Am. Chem. Soc. 135, 1882-1890 (2013).
29. Das, P. & Zhou, R. Urea-induced drying of carbon nanotubes suggests existence of a dry globule-like transient state during chemical denaturation of proteins. J. Phys. Chem. B 114, 5427-5430 (2010).
30. Fitch, B. G. et al. Blue Matter: Strong scaling of molecular dynamics on Blue Gene/L. 846-854 (Springe rBerlin Heidelberg, 2006).
31. Li, J. et al. Hydration and dewetting near graphite-CH(3) and graphite-COOH plates. J. Phys. Chem. B 109, 13639-13648 (2005).
32. Yang, Z., Wang, Z., Tian, X., Xiu, P. & Zhou, R. Amino acid analogues bind to carbon nanotube via pi-pi interactions: comparison of molecular mechanical and quantum mechanical calculations. J. Chem. Phys. 136, 025103, (2012).
33. Zuo, G., Kang, S. G., Xiu, P., Zhao, Y. & Zhou, R. Interactions Between Proteins and Carbon-Based Nanoparticles: Exploring the Origin of Nanotoxicity at the Molecular Level. Small 9, 1546-1556 (2013).
34. Humphrey, W., Dalke, A. & Schulten, K. VMD: Visual molecular dynamics. J. Mol. Graphics 14, 33-38 (1996).
35. Pettersen, E. F. et al. UCSF Chimera - A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
36. Kumar, S., Rosenberg, J. M., Bouzida, D., Swendsen, R. H. & Kollman, P. A. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13, 1011-1021 (1992).
37. Sahu, D., Debnath, P., Takayama, Y. & Iwahara, J. Redox properties of the A-domain of the HMGB1 protein. FEBS Lett. 582, 3973-3978 (2008).
38. Das, P., King, J. A. & Zhou, R. Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands. Proc. Natl. Acad. Sci. USA 108, 10514-10519 (2011).
39. Dai, B. et al. Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface. Proc. Natl. Acad. Sci. USA 110, 8543-8548 (2013).
40. Hua, L., Huang, X., Liu, P., Zhou, R. & Berne, B. J. Nanoscale dewetting transition in protein complex folding. J. Phys. Chem. B 111, 9069-9077 (2007).
41. Krone, M. G. et al. Role of water in mediating the assembly of Alzheimer amyloid-beta Abeta16-22 protofilaments. J. Am. Chem. Soc. 130, 11066-11072 (2008).
42. Ehrnhoefer, D. E. et al. Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Hum. Mol. Genet. 15, 2743-2751 (2006).
43. Ehrnhoefer, D. E. et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 15, 558-566 (2008).
44. Bieschke, J. et al. EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity. Proc. Natl. Acad. Sci. USA 107, 7710-7715 (2010).
45. Andrich, K. & Bieschke, J. in Natural Compounds as Therapeutic Agents for Amyloidogenic Diseases Vol. 863 Advances in Experimental Medicine and Biology (ed Neville, Vassallo) Ch. 7, 139-161 (Springer International Publishing, 2015).
46. Hub, J. S., De Groot, B. L. & Van Der Spoel, D. g-wham · A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates. J. Chem. Theory Comput. 6, 3713-3720 (2010).