Journal
CANADIAN JOURNAL OF CHEMISTRY
Volume 94, Issue 12, Pages 1090-1098Publisher
CANADIAN SCIENCE PUBLISHING, NRC RESEARCH PRESS
DOI: 10.1139/cjc-2016-0292
Keywords
glycoaminoglycans; heparin disaccharide; amyloid fibril; amyloid beta
Categories
Funding
- James and Esther King Biomedical Research Program of the Florida State Health Department (DOH) [08KN-11]
Ask authors/readers for more resources
In this computational study, we have combined molecular docking and molecular dynamics (MD) simulation techniques to explore interactions of monomeric and aggregated forms of Alzheimer's amyloid beta (A beta(40)) with seven chemically distinct heparin derived glycoaminoglycans (GAGs) referred to as ADC, SDC, DC, V1, V2, V3, and V4. The docking procedure proposed two major binding sites, i.e., one present at the top of the fibril (site A), and the other located in the hairpin region (site B). Due to its position, site B offers an interesting target to design molecules with anti-aggregation properties. Our results predicted that out of seven GAGs, only three of them (ADC, SDC, and DC) bind to site B. The identification of these molecules can advance our efforts to develop therapeutic interventions for this deadly disease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available