Chirality of the Disulfide in the Prion Proteins

Journal of Chemical Information and Computer Sciences

Volumn 44, Issue 1, 2004, Pages 286-288

  Carmack, Marvin ^a  

^a INDIANA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE BONDS; PRION PROTEINS;

AMINO ACIDS; CELLS; CHEMICAL BONDS; DISEASES; MOLECULAR STRUCTURE; NEUROLOGY; PATHOLOGY; X RAY CRYSTALLOGRAPHY;

PROTEINS;

DISULFIDE;

ARTICLE; CHEMISTRY; PRION; STEREOISOMERISM;

DISULFIDES; PRIONS; STEREOISOMERISM;

EID: 1542530869     PISSN: 00952338     EISSN: None     Source Type: Journal    
DOI: 10.1021/ci020073x     Document Type: Article

References (17)

1. The term Transmissible Spongiform Encephalopathies, or TSEs, also known as the prion diseases, includes scrapie in sheep; bovine spongiform encephalopathy (BSE) in cows, often referred to as "mad cow disease"; variant Creutzfeldt-Jacob disease in humans; kuru, in the Gore mountain people of New Guinea; chronic wasting disease in elk, deer, and various other animals; Gerstmann-Sträussler-Scheinker Disease (GSS) disease in humans; fatal familial insomnia (FFI) in humans. These are all diseases of the neural system involving gradual disintegration of the brain, loss of bodily functions, dementia, and ultimate death. They are characterized by long incubation periods between infection and the appearance of obvious symptoms. The infective agents appear to be misfolded forms of naturally occurring proteins. The mechanism(s) of the infective process are unknown and the subject of extensive investigation.
2. Knaus, K. J.; Morillas, M.; Swietnicki, W.; Malone, M.; Surewicz, W. K.; Yee, V. C. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nature Struct. Biol. 2001, 8(9), 770-774.
3. Zahn, R.; Liu, A.; Lührs, T.; Riek, R.; von Schroetter, C.; Garcia, F. L.; Billeter, R.; Calzolai, L.; Wider, G.; Wüthrich, K. NMR solution structure of the human prion protein. Proc. Nat. Acad. Sci. 2000, 97(1), 145-150.
4. Turk, E.; Teplow, D.; Hood, L. E.; Prusiner, S. B. Purification and properties of the cellular and scrapie hamster prion proteins. Eur. J. Biochem. 1988, 176, 21-23.
5. Maiti, N. R.; Surewicz, W. K. The role of the disulfide bridge in the folding and stability of the recombinant human prion protein. J. Biol. Chem. 2001, 276(4), 2427-2435.
6. Welker, E.; Raymond, L. D.; Scheraga, H. A.; Caughey, B. Intramolecular versus intermolecular bonds in prion proteins. B. J. Biol. Chem. 2002 (Sep 6), 277(36), 33477-33481.
7. Boyd, D. B. Conformational dependence of the electronic spectra in disulfides. J. Am. Chem. Soc. 1972, 94, 8799-8804.
8. Boyd, D. B. Electron redistribution in disulfide bonds under torsion. Theor. Chim. Acta 1973, 30, 137-150.
9. (a) Carmack, M.; Neubert, L. A. Circular dichroism and the absolute configuration of the chiral disulfide group. J. Am. Chem. Soc. 1967, 89, 7134-7136.
10. (b) Neubert, L. A.; Carmack, M. Circular dichroism of disulfides with dihedral angles of 0°, 30°, 60° in the 400-185 nm spectral region. J. Am. Chem. Soc. 1974, 96, 943-945.
11. de Laureto, P.; Scaramella, E.; de Filippis, V.; Marin, O.; Doni, M. G.; Fontana, A. Chemical synthesis and structural characterization of the RGB-protein decorsin: a potent inhibitor of platelet aggregation. Protein Sci. 1998, 7, 433-444.
12. Djerassi, C.; Wolf. H.; Bunnenberg, E. Optical rotatory dispersion studies. LXXVIII. Comparative studies of circular dichroism and rotatory dispersion curves. Some observations on sulfur-containing chromophores. J. Am. Chem. Soc. 1962, 84, 4552-61.
13. 30). Acta Crystallogr. 1977, B33, 962-969.
14. Zahn, R.; Liu, A.; Lührs, T.; Riek, R.; von Schroetter, C.; Garcia, F. L.; Billeter, M.; Calzolai, L.; Wider, G.; Wüthrich, K. NMR solution structure of the human prion protein. Proc. Nat. Acad. Sci. 2000, 97(1), 145-150.
15. Yam, P. The Pathological Protein. Mad Cow, Chronic Wasting, and Other Deadly Prion Diseases, 2003; 284 pages, Copernicus Books. An Imprint of Springer-Verlag: page 95ff.
16. Priola, S. A.; Chesebro, B.; Caughey, B. A View from the Top -Prion Diseases from 10,000 Feet. Science 2003, 300(5621), 917-921.
17. LeBlanc, A. C.; Roucou, X. Toxicity and Protection in Prions. Science 2003, 301(5630), 168-169.