Title

Authors

Affiliation

Department of Biotechnology and Bioinformatics, padmashree Dr.D.Y.Patil University, Belapur-400614, Navi Mumbai, India

Email

Ved.prakash2012@vit.ac.in; *Corresponding author

Article Type

Hypothesis

Date

Received August 28, 2014; Accepted August 31, 2014; Published September 30, 2014

The most common characteristics of diverse age-related neurodegenerative diseases are aggregation and accumulation of the misfolded protein in the brain. Alzheimer’s disease (AD) is one of these protein conformational diseases. Extracellular accumulation of amyloid β (Aβ) is one the neuropathological hallmarks of Alzheimer disease. Various studies have shown that mutation in specific hydrophobic region of Aβ protein inhibit the formation of β sheet, thus aggregation of this protein is stalled. The identification of such mutation in Aβ protein can help us in elucidating the etiology of sporadic Aβ. In our study we have selected three positions: 19ILU, 21ALA and 41ILU in Aβ protein based on their hydrophobic nature and substituted them with PRO ( βSheet breaker). The effects of the substitutions were analysed using molecular dynamics simulation studies. The results validated that the mutations in the specified regions change the hydrophobicity of the protein and the βsheet formation was declined to zero per cent.

Keywords

Alzheimer’s disease, Amyloid-beta precursor protein, Amyloid-beta peptide, Gromos, PPI-Pred, Argus Lab, UCSF Chimera.

Citation

Singh et al. Bioinformation 10(9): 569-574 (2014)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.