Molecular modeling on Zn(II) binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes

Science in China, Series B: Chemistry

Volumn 47, Issue 2, 2004, Pages 126-133

  Han, Daxiong ^a   Yang, Pin ^a  

^a SHANXI UNIVERSITY   (China)

Author keywords

Alzheimer's disease; Amyloid peptide; Binding mode; Molecular modeling; Zn(II)

Indexed keywords

NEUROLOGY; PATHOLOGY; PROTEINS; ZINC;

ALZHEIMER DISEASE; BINDING MODE; INSOLUBLE FIBRIL; MOLECULAR MODELING; PEPTIDE;

DISEASES;

EID: 3042761444     PISSN: 10069291     EISSN: None     Source Type: Journal    
DOI: 10.1360/03yb0163     Document Type: Article

References (14)

1. Storey, E., Cappai, R., The amyloid precursor protein of Alzheimer's disease and the Aβ peptide, Neuropathology and Applied Neurobiology, 1999, 25: 81-97.
2. Hasegawa, K., Yamaguchi, I., Omata, S. et al., Interaction between Aβ(l-42) and Aβ(l-40) in Alzheimer's β-amyloid fibril formation in vitro, Biochemistry, 1999, 38: 15514-15521.
3. Atwood, C. S., Martins, R. N., Smith, M. A. et al., Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins, Peptides, 2002, 23: 1343-1350.
4. Miura, T., Suzuki, K., Takeuchi, H. et al., Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes, Biochemistry, 2000, 39: 7024-7031.
5. Atwood, C. S., Scarpa, R. C., Huang, X. D. et al., Characterization of copper interactions with Alzheimer amyloid β-peptide: In-dentification of an attomolar-affinity copper binding site on amyloid β1-42, J. Neurochem., 2000, 75: 1219-1233.
6. 2+ inhibits the aggregation of amyloid β-peptide(l-42) in virtro, Angew. Chem. Int. Ed., 2001, 40: 2274-2277.
7. 2+ ions by a pentapeptide fragment present in the cysteine-rich region of amyloid precursor protein, J. Chem. Soc., Dalton Trans., 2002: 2266-2268.
8. Liu, S. T., Howlett, G., Barrow, C. J. et al., Histidine-13 Is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease, Biochemistry, 1999, 38: 9373-9378.
9. Atwood, C. S., Moir, R. D., Huang, X. et al., Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis, J. Biol. Chem., 1998, 273: 12817-12826.
10. Dong, J., Atwood, C. S., Anderson, V. E. et al., Metal binding and oxidation of amyloid P within isolated senile plaque cores: Raman microscopic Evidence, Biochemistry, 2003, 42: 2768-2773.
11. Morgan, D. M., Dong, J. J., Lynn, D. G. et al., Metal switch for amyloid formation: Insight into the structure of the nucleus, J. Am. Chem. Soc., 2002, 124: 12644-12645.
12. Hoops, S. C., Anderson, K. W., Merz, K. M., Force field design for metalloproteins, J. Am. Chem. Soc., 1991, 113: 8262-8270.
13. Coles, M., Bicknell, W., Watson, A. A. et al., Solution structure of amyloid beta-peptide(l-40) in a water-micelle environment, Is the membrance-spanning domain where we think it is? Biochemistry, 1998, 37: 11064-11077.
14. Roher, A. E., Chaney, M. O., Kuo, Y. M. et al., Morphology and toxicity of Aβ(1-42) dimmer derived from neuritic and vascular amyloid deposits of Alzheimer's disease, J. Biol. Chem., 1996, 271: 20631-20635.