Skip Navigation

Journal of Biochemistry 2006 139(4):733-740; doi:10.1093/jb/mvj083
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Chen, Y.R.
Right arrow Articles by Chen, Y.C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, Y.R.
Right arrow Articles by Chen, Y.C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

Regular Paper

The Effect of Aß Conformation on the Metal Affinity and Aggregation Mechanism Studied by Circular Dichroism Spectroscopy

Y.R. Chen1, H.B. Huang2, C.L. Chyan3, M.S. Shiao4, T.H. Lin4,5,6,* and Y.C. Chen1,7,*

1 Institute of Medical Science, Tzu Chi University, Hualien, Taiwan; 2 Institute of Molecular Biology, National Chung-Cheng University, Chiayi, Taiwan; 3 Department of Chemistry, National Duan-Hwa University, Hualien, Taiwan; 4 Department of Medical Research and Education, Taipei Veterans General Hospital, Shihpai, Taipei, Taiwan; 5 Institute of Biochemistry and 6 Institute of Bioinformatics and Structural Biology Program, National Yang-Ming University, Shihpai, Taipei, Taiwan; and 7 Department of Medical Technology, Tzu Chi University, Hualien, Taiwan

* To whom correspondence should be addressed at: Department of Medical Technology, Tzu Chi University, Hualien 970, Taiwan. Fax: +886-3-8571917, E-mail: chen15{at}mail.tcu.edu.tw (Y.C. Chen); Department of Medical Research & Education, Taipei Veterans General Hospital, Teipei, Taiwan. E-mail: thlin@vghtpe.gov.tw (T.H. Lin).

The conformational change and associated aggregation of ß amyloid (Aß) with or without metals is the main cause of Alzheimers' disease (AD). In order to further understand the effects of Aß and its associated metals on the aggregation mechanism, the influence of Aß conformation on the metal affinity and aggregation was investigated using circular dichroism (CD) spectroscopy. The Aß conformation is dependent on pH and trifluoroethanol (TFE). The binding of metals to Aß was found to be dependent on the Aß conformation. The aggregation induced by Aß itself or its associated metals is completely diminished for Aß in 40% TFE. Only in 5% and 25% TFE can Aß undergo an {alpha}-helix to ß-sheet aggregation, which involve a three-state mechanism for the metal-free state, and a two-state transition for the metal-bound state, respectively. The aggregation-inducing activity of metals is in the order, Cu2+ > Fe3+ ≥ Al3+ > Zn2+.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
T. Ariga, M. P. McDonald, and R. K. Yu
Thematic Review Series: Sphingolipids. Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease--a review
J. Lipid Res., June 1, 2008; 49(6): 1157 - 1175.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
J. Ikebe, N. Kamiya, J.-I. Ito, H. Shindo, and J. Higo
Simulation study on the disordered state of an Alzheimer's beta amyloid peptide Abeta(12 36) in water consisting of random-structural, beta-structural, and helical clusters
Protein Sci., August 1, 2007; 16(8): 1596 - 1608.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.