Structure and dynamics of self-assembled poly(ethylene glycol) based coiled-coil nano-objects

ChemPhysChem

Volumn 5, Issue 4, 2004, Pages 488-494

  Vandermeulen, Guido W M ^a   Hinderberger, Dariush ^a   Xu, Hui ^c   Sheiko, Sergei S ^c   Jeschke, Gunnar ^a   Klok, Harm Anton ^b  

^a MAX PLANCK INSTITUTE FOR POLYMER RESEARCH   (Germany)

^b EPFL   (Switzerland)

^c University of North Carolina at Chapel Hill   (United States)

Author keywords

Block copolymers; EPR spectroscopy; Peptides; Scanning probe microscopy; Self assembly

Indexed keywords

BLOCK COPOLYMERS; ETHYLENE GLYCOL; MICA; PARAMAGNETIC RESONANCE; PEPTIDES; POLYETHYLENE GLYCOLS; POLYETHYLENE OXIDES; POLYOLS; SCANNING PROBE MICROSCOPY; SELF ASSEMBLY;

AMINO ACID SEQUENCE; ELECTRON PARAMAGNETIC RESONANCES (EPR); EPR SPECTROSCOPY; HYBRID BLOCK COPOLYMERS; NANOSIZED OBJECTS; PARALLEL ALIGNMENTS; STRUCTURE AND DYNAMICS; SUPRAMOLECULAR MATERIALS;

ELECTRON SPIN RESONANCE SPECTROSCOPY;

COPOLYMER; MACROGOL; PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; DYNAMICS; ELECTRON SPIN RESONANCE; MUTATION; PARTICLE SIZE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 2442532695     PISSN: 14394235     EISSN: None     Source Type: Journal    
DOI: 10.1002/cphc.200301079     Document Type: Article

References (33)

1. a) S. Förster, T. Plantenberg, Angew. Chem. 2002, 114, 712-739; Angew. Chem. Int. Ed. 2002, 41, 688-714;
2. a) S. Förster, T. Plantenberg, Angew. Chem. 2002, 114, 712-739; Angew. Chem. Int. Ed. 2002, 41, 688-714;
3. b) I. W. Hamley, Angew. Chem. 2003, 115, 1730-1752; Angew. Chem. Int. Ed. 2003, 42, 1692-1712.
4. b) I. W. Hamley, Angew. Chem. 2003, 115, 1730-1752; Angew. Chem. Int. Ed. 2003, 42, 1692-1712.
5. H.-A. Klok, Angew. Chem. 2002, 114, 1579-1583; Angew. Chem. Int. Ed. 2002, 41, 1509-1513.
6. H.-A. Klok, Angew. Chem. 2002, 114, 1579-1583; Angew. Chem. Int. Ed. 2002, 41, 1509-1513.
7. a) O. Rathore, D. Y. Sogah, J. Am. Chem. Soc. 2001, 123, 5231-5239;
8. b) T. S. Burkoth, T. L. S. Benzinger, D. N. M. Jones, K. Hallenga, S. C. Meredith, D. G. Lynn, J. Am. Chem. Soc. 1998, 120, 7655-7656;
9. c) T. S. Burkoth, T. L. S. Benzinger, V. Urban, D. G. Lynn, S. C. Meredith, P. Thiyagarajan, J. Am. Chem. Soc. 1999, 121, 7429-7430;
10. d) A. Rösler, H.-A. Klok, I. W. Hamley, V. Castelletto, O. O. Mykhaylyk, Biomacromolecules 2003, 4, 859-863.
11. G. W. M. Vandermeulen, C. Tziatzios, H.-A. Klok, Macromolecules 2003, 36, 4107-4114.
12. The heptad repeat sequence used for the peptide segment is "a-g": LAEIEAK This amino acid sequence is anticipated to form parallel α-helical coiled coils, because the interhelical electrostatic interactions are attractive when oriented in parallel fashion and repulsive when oriented antiparallel. See for example, O. D. Monera, N. E. Zhou, C. M. Kay, R. S. Hodges, J. Biol. Chem. 1993, 268, 19218-19227.
13. a) Biological Magnetic Resonance, Vol. 19 (Eds.: L. J. Berliner, S. S. Eaton, G. R. Eaton), Kluwer, Amsterdam, 2001;
14. b) A. D. Milov, A. G. Maryasov, Y. D. Tsvetkov, Appl. Magn. Reson. 1998, 15, 107-143;
15. c) G. Jeschke, Macromol. Rapid Commun. 2002, 23, 227-246;
16. d) R. G. Larsen, D. J. Singel, J. Chem. Phys. 1993, 98, 5134-5146;
17. e) R. E. Martin, M. Pannier, F. Diederich, V. Gramlich, M. Hubrich, H.W. Spiess, Angew. Chem. 1998, 110, 2994-2998; Angew. Chem. Int. Ed. 1998, 37, 2834-2837;
18. e) R. E. Martin, M. Pannier, F. Diederich, V. Gramlich, M. Hubrich, H.W. Spiess, Angew. Chem. 1998, 110, 2994-2998; Angew. Chem. Int. Ed. 1998, 37, 2834-2837;
19. f) A. Weber, O. Schiemann, B. Bode, T. F. Prisner, J. Magn. Reson. 2002, 157, 277-285.
20. g) C. Elsasser, M. Brecht, R. Bittl, J. Am. Chem. Soc. 2002, 124, 12606-12611.
21. P. G. Fajer in Encyclopedia of Analytical Chemistry (Ed.: R. Meyers) Wiley and Sons, London, 2000, pp. 5725-5761.
22. W. L. Hubbell, C. Altenbach, Curr. Opin. Struct. Biol. 1994, 4, 566-573.
23. J. Y. Su, R. S. Hodges, C. M. Kay, Biochemistry 1994, 33, 15501-15510.
24. G. Jeschke, A. Koch, U. Jonas, A. Godt, J. Magn. Reson. 2002, 155, 72-82.
25. a) M. Pannier, S. Veit, A. Godt, G. Jeschke, H. W. Spiess, J. Magn. Reson. 2000, 142, 331-340;
26. b) G. Jeschke, ChemPhysChem 2002, 3, 927-932.
27. G. Jeschke, G. Panek, A. Godt, A. Bender, H. Paulsen, Appl. Magn. Reson., in press.
28. The peptide contains 23 amino acids and the spin label is attached to the C-terminal tyrosine residue. In a normal α-helix, one turn contains 3.6 residues and has a distance of 5.4 Å. The amino acids are thus separated 1.5 Å through space (23 x 1.5 Å = 3.45 nm). If the peptide chains would be oriented in antiparallel fashion, the spin labels would be ≈ 3.45 nm apart. In a coiled coil, however, a helix turn contains only 3. 5 residues and therefore the amino acids are separated a little less than 1.5 Å. This difference is however very small.
29. Recording EPR data from the unimer peptide or mPEG(750) block copolymer samples in PBS/glycerol is not feasible as one would have to dilute the solutions to such an extent that the self-assembly equilibrium is shifted far to the unimer side. This corresponds to spin label concentrations below the detection limit. Samples of the free spin probe were measured under the same conditions as the spin-labeled peptide and diblock copolymer samples.
30. D. J. Schneider, J. H. Freed in Biological Magnetic Resonance, VoL 8 (Eds.: L. J. Berliner, J. Reuben), Plenum Press, New York, 1989, Chap. 1.
31. S.A. Zager, J. H. Freed, J. Chem. Phys. 1982, 77, 3344-3359.
32. H. Gehrhardt, M. Mutter, Polym. Bull. 1987, 18, 487-492.
33. UV/Vis spectroscopic analysis of the solutions used for EPR spectroscopy revealed sample concentrations of 290 μM for the peptide and 810 μM for the mPEG(750) block copolymer.