Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
Peptides
Year: 2009  |  Volume: 30  |  Issue: 7  |  Page No.: 1282 - 1287

Hybrid peptides attenuate cytotoxicity of β-amyloid by inhibiting its oligomerization: Implication from solvent effects

Xun Sun, Wei-hui Wu, Qian Liu, Mei-sha Chen, Ye-ping Yu, Ying Ma, Yu-fen Zhao and Yan-mei Li    

Abstract:

Abnormal assembly of monomeric β-amyloid (Aβ) in Alzheimer's disease leads to the formation of most neurotoxic oligomers in vivo. In this study, we explored a linking strategy to design hybrid peptides, by combining the Aβ recognition motif and the solvent disruptive sequences. We found that in vitro all synthetic peptides with the recognition motif can affect Aβ fibrillization and alter the morphology of Aβ aggregates variously, different from those without the recognition motif. The effects of peptides containing recognition motif on Aβ aggregation correlate with their abilities to change the surface tension of solutions. In addition, compounds with the recognition motif, not those without such motif, can inhibit cytotoxicity of Aβ in cell culture probably by decreasing the amount of toxic Aβ oligomers. These results indicate that recognition domain and solvent effect should be considered as important factors when designing molecules to target Aβ aggregation.

View Fulltext    |   Related Articles   |   Back
 
 
   
 
 
 
  Related Articles

No Article Found
 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility