Organization of designed nanofibrils assembled from α-helical peptides as determined by electron microscopy

Journal of Peptide Science

Volumn 10, Issue 5, 2004, Pages 291-297

  Kajava, Andrey V ^a,e   Potekhin, Sergey A ^b   Corradin, Giampietro ^c   Leapman, Richard D ^d  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^c UNIVERSITY OF LAUSANNE   (Switzerland)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

^e Centre National de la Recherche Scientifique   (France)

Author keywords

helical coiled coil; Design; Fibrils; Peptides; Self assembly

Indexed keywords

DIMER; PEPTIDE;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; FIBER; MASS; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; SCANNING TRANSMISSION ELECTRON MICROSCOPY; STAINING;

MICROSCOPY, ELECTRON, SCANNING; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 2342555690     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.520     Document Type: Article

References (22)

1. Whitesides GM, Boncheva M. Beyond molecules: self-assembly of mesoscopic and macroscopic components. Proc. Natl Acad. Sci USA 2002; 99: 4769-4774.
2. Lowe CR. Nanobiotechnology: the fabrication and applications of chemical and biological nanostructures. Curr. Opin. Struct. Biol. 2000; 10: 428-434.
3. Reinhoudt DN, Crego-Calama M. Synthesis beyond the molecule. Science 2002; 295: 2403-2407.
4. Marini DM, Hwang W, Lauffenburger DA, Zhang S, Kamm RD. Left-handed helical ribbon intermediates in the self-assembly of a b-sheet peptide. Nano Lett. 2002; 2: 295-299.
5. Vauthey S, Santoso S, Gong H, Watson N, Zhang S. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc. Natl Acad. Sci. USA 2002; 99: 5355-5360.
6. Hartgerink JD, Beniash E, Stupp SI. Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self assembling materials. Proc. Natl Acad. Sci. USA 2002; 99: 5133-5138.
7. Pandya MJ, Spooner GM, Sunde M, Thorpe JR, Rodger A, Woolfson DN. Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis. Biochemistry 2000; 39: 8728-8734.
8. Ogihara NL, Ghirlanda G, Bryson JW, Gingery M, DeGrado WF, Eisenberg D. Design of three-dimensional domain-swapped dimers and fibrous oligomers. Proc. Natl Acad. Sci. USA 2001; 98: 1404-1409.
9. Potekhin SA, Melnik TN, Popov V, Lanina NF, Vazina AA, Rigler P, Verdini AS, Corradin G, Kajava AV. De novo design of fibrils made of short alpha-helical coiled coil peptides. Chem. Biol. 2001; 8: 1025-1032.
10. Pack P, Pluckthun A. Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli. Biochemistry 1992; 31: 1579-1584.
11. Terskikh AV, Le Doussal JM, Crameri R, Fisch I, Mach JP, Kajava AV. 'Peptabody': a new type of high avidity binding protein. Proc. Natl Acad. Sci. USA 1997; 94: 1663-1668.
12. Wall JS, Hainfeld JF. Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Biophys. Chem. 1986; 15: 355-376.
13. Engel A, Baumeister W, Saxton WO. Mass mapping of a protein complex with the scanning transmission electron microscope. Proc. Natl Acad. Sci. USA 1982: 79: 4050-4054.
14. Jaenicke L. A rapid micromethod for the determination of nitrogen and phosphate in biological material. Anal. Biochem 1974; 61: 623-627.
15. Leapman RD, Gallant PE, Reese TS, Andrews SB. Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy. Proc. Natl Acad. Sci. USA 1997; 94: 7820-7824.
16. Antzutkin ON, Leapman RD, Balbach JJ, Tycko R. Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 2002; 41: 15 436-15 450.
17. Leapman RD, Andrews SB. Characterization of biological macromolecules by combined mass mapping and electron energy-loss spectroscopy. J. Microsc. 1992; 165: 225-238.
18. Dayring HE, Tramonato A, Sprang SR, Fletterick RJ. Interactive program for visualization and modelling of proteins, nucleic acids and small molecules. J. Mol. Graphics 1986; 4: 82-87.
19. Kajava AV. Modeling of a five-stranded coiled coil structure for the assembly domain of the cartilage oligomeric matrix protein. Proteins 1996; 24: 218-226.
20. Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? Science 1996; 274: 761-765.
21. O'Shea EK, Klemm JD, Kim PS, Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 1991; 254: 539-544.
22. Harbury PB, Zhang T, Kim PS, Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 1993; 262: 1401-1407.