PL EN


Preferences help
enabled [disable] Abstract
Number of results
2012 | 122 | 2 | 279-283
Article title

De Novo Designed Proteins - Perspective Materials for Nanotechnology

Authors
Content
Title variants
Languages of publication
EN
Abstracts
EN
The paper explores the field of de novo protein design, as a source of material for effective hybrid nanostructures. Main design approaches, namely the intuitional and the computational strategy, are briefly overviewed. The achievements in the field are illustrated with several examples, starting from historical heme binding maquettes to novel non-natural enzymes. Separate paragraph covers the problem of designing peptides, which may act as anchor between biological and non-biological parts of nanostructures. The advantages of de novo designed proteins and still existing problems of the field are discussed.
Keywords
EN
Publisher

Year
Volume
122
Issue
2
Pages
279-283
Physical description
Dates
published
2012-08
Contributors
author
  • Laboratory of Biological Physics, Institute of Physics, Polish Academy of Sciences, al. Lotników 32/46, 02-668 Warsaw, Poland
References
  • 1. P. Marguet, F. Balagadde, C. Tan, L. You, J. Royal Society Interface 4, 607 (2007)
  • 2. S. Mackowski, J. Phys., Condens. Matter 22, 193102 (2010)
  • 3. G. Grigoryan, Y.H. Kim, R. Acharya, K. Axelrod, R.M. Jain, L. Willis, M. Drndic, J.M. Kikkawa, W.F. DeGrado, Science 332, 1071 (2011)
  • 4. D.E. Robertson, R.S. Farid, C.C. Moser, J.L. Urbauer, S.E. Mulholland, R. Pidikiti, J.D. Lear, A.J. Wand, W.F. DeGrado, P.L. Dutton, Nature 368, 425 (1994)
  • 5. J.R. Beasley, M.H. Hecht, J. Biol. Chem. 272, 2031 (1997)
  • 6. B.A. Smith, M.H. Hecht, Curr. Opinion Chem. Biol. 15, 421 (2011)
  • 7. J. Garnier, J.F. Gibrat, B. Robson, Methods Enzymol. 266, 540 (1996)
  • 8. C. Cole, J.D. Barber, G.J. Barton, Nucl. Acids Res. 36, W197 (2008)
  • 9. P.B. Harbury, J.J. Plecs, B. Tidor, T. Alber, P.S. Kim, Science 282, 1462 (1998)
  • 10. M.J.I. Andrews, A.B. Tabor, Tetrahedron 55, 11711 (1999)
  • 11. V. Nanda, R.L. Koder, Nature Chem. 2, 15 (2010)
  • 12. R.L. Koder, J.L. Anderson, L.A. Solomon, K.S. Reddy, C.C. Moser, P.L. Dutton, Nature 458, 305 (2009)
  • 13. D. Noy, P.L. Dutton, Biochemistry 45, 2103 (2006)
  • 14. I. Cohen-Ofri, M. van Gastel, J. Grzyb, A. Brandis, I. Pinkas, W. Lubitz, D. Noy, J. Am. Chem. Soc. 133, 9526 (2011)
  • 15. J. Grzyb, F. Xu, L. Weiner, E.J. Reijerse, W. Lubitz, V. Nanda, D. Noy, Biochim. Biophys. Acta 1797, 406 (2010)
  • 16. C.M. Kraemer-Pecore, A.M. Wollacott, J.R. Desjarlais, Curr. Opinion Chem. Biol. 5, 690 (2001)
  • 17. B.R. Gibney, S.E. Mulholland, F. Rabanal, P.L. Dutton, Proc. Natl. Acad. Sci. 93, 15041 (1996)
  • 18. V. Nanda, M.M. Rosenblatt, A. Osyczka, H. Kono, Z. Getahun, P.L. Dutton, J.G. Saven, W.F. DeGrado, J. Am. Chem. Soc. 127, 5804 (2005)
  • 19. F. Rabanal, B.R. Gibney, W.F. DeGrado, C.C. Moser, P. Leslie Dutton, Inorg. Chim. Acta 243, 213 (1996)
  • 20. D. Noy, B.M. Discher, I.V. Rubtsov, R.M. Hochstrasser, P.L. Dutton, Biochemistry 44, 12344 (2005)
  • 21. J. Grzyb, F. Xu, R. Łuczkowska, E.J. Reijerse, W. Lubitz, V. Nanda, D. Noy, Biochim Biophys Acta - Bioenergetics 1817, 1256 (2012)
  • 22. A. Zouzoulas, A.G. Therien, R. Scanzano, C.M. Deber, R. Blostein, J. Biol. Chem. 278, 40437 (2003)
  • 23. L.L. Freeman-Cook, D. DiMaio, Oncogene 24, 7756 (2005)
  • 24. B.M. Discher, D. Noy, J. Strzalka, S. Ye, C.C. Moser, J.D. Lear, J.K. Blasie, P.L. Dutton, Biochemistry 44, 12329 (2005)
  • 25. P. Barth, B. Wallner, D. Baker, PNAS 106, 1409 (2009)
  • 26. R. Sterner, F.X. Schmid, Science 304, 1916 (2004)
  • 27. B. Schreier, C. Stumpp, S. Wiesner, B. Höcker, Proc. Natl. Acad. Sci. 106, 18491 (2009)
  • 28. M.A. Dwyer, L.L. Looger, H.W. Hellinga, Science 304, 1967 (2004)
  • 29. J. Kaplan, W.F. DeGrado, PNAS 101, 11566 (2004)
  • 30. I.V. Korendovych, D.W. Kulp, Y. Wu, H. Cheng, H. Roder, W.F. DeGrado, Proc. Natl. Acad. Sci. 108, 6823 (2011)
  • 31. L. Jiang, E.A. Althoff, F.R. Clemente, L. Doyle, D. Rothlisberger, A. Zanghellini, J.L. Gallaher, J.L. Betker, F. Tanaka, C.F. Barbas, 3rd, D. Hilvert, K.N. Houk, B.L. Stoddard, D. Baker, Science 319, 1387 (2008)
  • 32. D. Rothlisberger, O. Khersonsky, A.M. Wollacott, L. Jiang, J. DeChancie, J. Betker, J.L. Gallaher, E.A. Althoff, A. Zanghellini, O. Dym, S. Albeck, K.N. Houk, D.S. Tawfik, D. Baker, Nature 453, 190 (2008)
  • 33. L. Yuan, I. Kurek, J. English, R. Keenan, Microbiol. Mol. Biol. Rev. 69, 373 (2005)
  • 34. S.M. Lippow, B. Tidor, Curr. Opin. Biotechnol. 18, 305 (2007)
  • 35. A.L. Pinto, H.W. Hellinga, J.P. Caradonna, Proc. Natl. Acad. Sci. 94, 5562 (1997)
  • 36. M.K. DiTursi, S.-J. Kwon, P.J. Reeder, J.S. Dordick, Protein Eng. Design Select. 19, 517 (2006)
  • 37. Y. Liu, B. Kuhlman, Nucl. Acids Res. 34, W235 (2006)
  • 38. P.-S. Huang, Y.-E.A. Ban, F. Richter, I. Andre, R. Vernon, W.R. Schief, D. Baker, PLoS ONE 6, e24109 (2011)
  • 39. A.D. Keefe, J.W. Szostak, Nature 410, 715 (2001)
  • 40. K. Jomova, M. Valko, Toxicology 283, 65 (2011)
  • 41. B. Debasis, D. Bern, L. Qian, P.H. Holloway, J. Phys. D 41, 182002 (2008)
  • 42. I.L. Medintz, T. Pons, S.A. Trammell, A.F. Grimes, D.S. English, J.B. Blanco-Canosa, P.E. Dawson, H. Mattoussi, J. Am. Chem. Soc. 130, 16745 (2008)
  • 43. B.R. Peelle, E.M. Krauland, K.D. Wittrup, A.M. Belcher, Langmuir 21, 6929 (2005)
  • 44. C.K. Thai, H. Dai, M.S. Sastry, M. Sarikaya, D.T. Schwartz, F. Baneyx, Biotech. Bioeng. 87, 129 (2004)
  • 45. S.R. Whaley, D.S. English, E.L. Hu, P.F. Barbara, A.M. Belcher, Nature 405, 665 (2000)
  • 46. T. Hayashi, K. Sano, K. Shiba, Y. Kumashiro, K. Iwahori, I. Yamashita, M. Hara, Nano Lett. 6, 515 (2006)
  • 47. E.E. Oren, C. Tamerler, M. Sarikaya, Nano Lett. 5, 415 (2005)
  • 48. U.O. Seker, B. Wilson, S. Dincer, I.W. Kim, E.E. Oren, J.S. Evans, C. Tamerler, M. Sarikaya, Langmuir 23, 7895 (2007)
  • 49. M. Sarikaya, C. Tamerler, A.K. Jen, K. Schulten, F. Baneyx, Nature Mater. 2, 577 (2003)
  • 50. C. Tamerler, D. Khatayevich, M. Gungormus, T. Kacar, E.E. Oren, M. Hnilova, M. Sarikaya, Biopolymers 94, 78 (2010)
  • 51. M. Gungormus, M. Branco, H. Fong, J.P. Schneider, C. Tamerler, M. Sarikaya, Biomaterials 31, 7266 (2010)
  • 52. L. Song, Y. Liu, Z. Zhang, X. Wang, J. Chen, Prot. J. 29, 516 (2010)
  • 53. M.-K. Liang, O. Deschaume, S.V. Patwardhan, C.C. Perry, J. Mater. Chem. 21, 80 (2011)
  • 54. S. Singh, K. Bozhilov, A. Mulchandani, N. Myung, W. Chen, Chem. Commun. 46, 1473 (2010)
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-appv122n2p08kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.