Protein Misfolding and Amyloid Formation in Alzheimer’s Disease

Abstract

The information necessary for proteins to correctly fold into biologically active three dimensional (3D) structures is present in the amino acid sequence. The ways by which proteins fold still remain one of the unexplained mysteries in the field of protein biochemistry. Investigating the impact and consequences of protein misfolding can help decipher the molecular causes behind the complex amyloid diseases such as Alzheimer’s disease (AD) and Parkinson’s disease. Various participating molecular entities like amyloid beta (Aβ), tau protein, and non-beta sheets are facilitating the pathogenesis of Alzheimer’s disease. Understanding their structure as well as their mechanism of action is useful to decode the therapeutic treatment for these complex diseases.

Keywords

Protein misfolding Amyloid formation Amyloid beta structure Amyloid fibrils Alzheimer’s disease Neurodegenerative disorders 

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Copyright information

© Springer India 2015

Authors and Affiliations

  • Iftikhar Aslam Tayubi
    • 1
  • Ahmad Firoz
    • 2
    • 3
  • Adeel Malik
    • 4
  1. 1.Faculty of Computing and Information TechnologyKing Abdulaziz UniversityRabighKingdom of Saudi Arabia
  2. 2.School of Chemistry and BiochemistryThapar UniversityPatialaIndia
  3. 3.Biomedical Informatics Center of ICMRPost Graduate Institute of Medical Education and Research (PGIMER)ChandigarhIndia
  4. 4.Perdana University Centre for Bioinformatics (PU-CBi), MARDI ComplexJalan MAEPS PerdanaSerdangMalaysia

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