Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP

Nature Chemistry

Volumn 5, Issue 7, 2013, Pages 613-620

  Biswas, Shuvendu ^a   Kinbara, Kazushi ^b   Niwa, Tatsuya ^c   Taguchi, Hideki ^c   Ishii, Noriyuki ^d   Watanabe, Sumiyo ^e   Miyata, Kanjiro ^e   Kataoka, Kazunori ^a,e   Aida, Takuzo ^a,f  

^a UNIVERSITY OF TOKYO   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^d NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^e UNIVERSITY OF TOKYO   (Japan)

^f RIKEN Center for Emergent Matter Science   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GREEN FLUORESCENT PROTEIN; MAGNESIUM; NANOMATERIAL;

ARTICLE; CHEMISTRY; HYDROLYSIS; METABOLISM; PROTEIN CONFORMATION; ROBOTICS; TRANSMISSION ELECTRON MICROSCOPY;

ADENOSINE TRIPHOSPHATE; GREEN FLUORESCENT PROTEINS; HYDROLYSIS; MAGNESIUM; MICROSCOPY, ELECTRON, TRANSMISSION; NANOSTRUCTURES; PROTEIN CONFORMATION; ROBOTICS;

EID: 84879374122     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1681     Document Type: Article

References (39)

1. Freitas, R. A. What is nanomedicine? Nanomed. Nanotechnol. Biol. Med. 1, 2-9 (2005).
2. Kinbara, K. & Aida, T. Toward intelligent molecular machines: directed motions of biological and artificial molecules and assemblies. Chem. Rev. 105, 1377-1400 (2005).
3. Corpvan den Heuvel, M. G. L. & Dekker, C. Motor proteins at work for nanotechnology. Science 317, 333-336 (2007).
4. Schliwa, M. (ed.) Molecular Motors (Wiley-VCH, 2003).
5. Youell, J. & Firman, K. Biological molecular motors for nanodevices. Nanotechnol. Percept. 3, 75-96 (2007).
6. ′-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation. Pharmacol. Ther. 112, 358-404 (2006).
7. Mal, N. K., Fujiwara, M. & Tanaka, Y. Photocontrolled reversible release of guest molecules from coumarin-modified mesoporous silica. Nature 421, 350-353 (2003).
8. Modi, S. et al. A DNA nanomachine that maps spatial and temporal pH changes inside living cells. Nature Nanotech. 4, 325-330 (2009).
9. Zhu, C. L., Lu, C. H., Song, X. Y., Yang, H. H. & Wang, X. R. Bioresponsive controlled release using mesoporous silica nanoparticles capped with aptamer-based molecular gate. J. Am. Chem. Soc. 133, 1278-1281 (2011).
10. Naito, M. et al. A phenylboronate functionalized polyion complex micelle for ATP-triggered release of siRNA. Angew. Chem. Int. Ed. 51, 10751-10755 (2012).
11. King, W., Pytel, N., Ng, K. & Murphy, W. Triggered drug release from dynamic microspheres via a protein conformational change. Macromol. Biosci. 10, 580-584 (2010).
12. Hartl, F. U., Bracher, A. & Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature475, 324-332 (2011).
13. Biswas, S. et al. A tubular biocontainer: metal ion-induced 1D assembly of a molecularly engineered chaperonin. J. Am. Chem. Soc. 131, 7556-7557 (2009).
14. De Greef, T. F. A. et al. Supramolecular polymerization. Chem. Rev. 109, 5687-5754 (2009).
15. Aida, T., Meijer, E. W. & Stupp, S. I. Functional supramolecular polymers. Science 335, 813-817 (2012).
16. Wang, X. et al. Cylindrical block copolymer micelles and co-micelles of controlled length and architecture. Science 317, 644-647 (2007).
17. Zhang, W. et al. Supramolecular linear heterojunction composed of graphite-like semiconducting nanotubular segments. Science 334, 340-343 (2011).
18. Okuda, H. et al. The intermediate domain defines broad nucleotide selectivity for protein folding in Chlamydophila GroEL1. J. Biol. Chem. 283, 9300-9307 (2008).
19. Roseman, A. M., Chen, S., White, H., Braig, K. & Saibil, H. R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87, 241-251 (1996).
20. Makino, Y., Amada, K., Taguchi, H. & Yoshida, M. Chaperonin-mediated folding of green fluorescent protein. J. Biol. Chem. 272, 12468-12474 (1997).
21. Frank, G. A. et al. Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations. Proc. Natl Acad. Sci. USA 107, 6270-6274 (2010).
22. Yifrach, O. & Horovitz, A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308 (1995).
23. Gray, T. E. & Fersht, A. R. Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 292, 254-258 (1991).
24. Gribble, F. M. et al. A novel method for measurement of submembrane ATP concentration. J. Biol. Chem. 275, 30046-30049 (2000).
25. Gorman, M. W., Feigl, E. O. & Buffington, C. W. Human plasma ATP concentration. Clin. Chem. 53, 318-325 (2007).
26. Ellis, G. A., Palte, M. J. & Raines, R. T. Boronate-mediated biologic delivery. J. Am. Chem. Soc. 134, 3631-3634 (2012).
27. Otsuka, H., Uchimura, E., Koshino, H., Okano, T. & Kataoka, K. Anomalous binding profile of phenylboronic acid with N-acetylneuraminic acid (Neu5Ac) in aqueous solution with varying pH. J. Am. Chem. Soc. 125, 3493-3502 (2003).
28. Shimizu, A. et al. The region of alpha-lactalbumin recognized by GroEL. J. Biochem. 124, 319-325 (1998).
29. Makio, T., Arai, M. & Kuwajima, K. Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES. J. Mol. Biol. 293, 125-137 (1999).
30. Lim, Y. B. et al. A cyclic RGD-coated peptide nanoribbon as a selective intracellular nanocarrier. Org. Biomol. Chem. 6, 1944-1948 (2008).
31. Kim. Y., Choi, Y., Weissleder, R. & Tung, C. H. Membrane permeable esterase-activated fluorescent imaging probe. Bioorg. Med. Chem. Lett. 17, 5054-5057 (2007).
32. Tian, L. et al. Selective esterase-ester pair for targeting small molecules with cellular specificity. Proc. Natl Acad. Sci. USA 109, 4756-4761 (2012).
33. Geng, Y. et al. Shape effects of filaments versus spherical particles in flow and drug delivery. Nature Nanotech. 2, 249-255 (2007).
34. Ferrari, M. Cancer nanotechnology: opportunities and challenges. Nature Rev. Cancer 5, 161-171 (2005).
35. Ishii, D. et al. Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles. Nature 423, 628-632 (2003).
36. Pellegatti, P. et al. Increased level of extracellular ATP at tumor sites: in vivo imaging with plasma membrane luciferase. PLoS ONE 3, e2599 (2008).
37. Motojima, F. et al. Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding. Biochem. Biophys. Res. Commun. 267, 842-849 (2000).
38. Sakata, T., Yan, Y. & Marriott, G. Family of site-selective molecular optical switches. J. Org. Chem. 70, 2009-2013 (2005).
39. ′- dithiodipyridine. Anal. Bioanal. Chem. 373, 266-276 (2002).