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Structure modeling and dynamics driven mutation and phosphorylation analysis of Beta-amyloid peptides.

Singh SK, Singh A, Prakash V, C SK - Bioinformation (2014)

Bottom Line: 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.

View Article: PubMed Central - PubMed

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

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus

Amyloid Beta sequence and structure
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC4209365&req=5

Figure 1: Amyloid Beta sequence and structure

Mentions: Solution NMR structure PDB 1IYT was taken from the RCSBProtein Data and employed as starting configurations for theMD simulations and other analysis (Figure 1).


Structure modeling and dynamics driven mutation and phosphorylation analysis of Beta-amyloid peptides.

Singh SK, Singh A, Prakash V, C SK - Bioinformation (2014)

Amyloid Beta sequence and structure
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4209365&req=5

Figure 1: Amyloid Beta sequence and structure
Mentions: Solution NMR structure PDB 1IYT was taken from the RCSBProtein Data and employed as starting configurations for theMD simulations and other analysis (Figure 1).

Bottom Line: 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.

View Article: PubMed Central - PubMed

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

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus