Protein Misfolding vs. Alzheimer Disease
Folding Conformations of Amyloid Beta-42

  • The major components of neurotic plaques found in Alzheimer Disease (AD) are peptides known as amyloid beta-peptides (A-beta-42).
  • In vitro amyloid beta-peptides may undergo a conformational transition from a soluble form to aggregated fibrillary b-sheet structures, which seem to be neurotoxic.
  • Conformational studies on these peptides in aqueous solution are complicated by their tendency to aggregate.
  • Compare the NMR conformers of A-beta-(1-42) of 1Z0Q and 1IYT in aqueous media to reveal the misfolding, alpha-to-beta conformational transition

Reference:

  • Orlando Crescenzi, Simona Tomaselli, Remo Guerrini, Severo Salvadori, Anna M. D’Ursi, Piero Andrea Temussi and Delia Picone, Solution structure of the Alzheimer amyloid b-peptide (1–42) in an apolar microenvironment, 2002; Eur. J. Biochem. 269,5642–5648.
  • .Simona Tomaselli, Veronica Esposito, Paolo Vangone, Nico A. J. van Nuland, Alexandre M. J. J. Bonvin, Remo Guerrini, Teodorico Tancredi, Piero A. Temussi, and Delia Picone,The a-to-b Conformational Transition of Alzheimer’s Ab-(1–42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of b Conformation Seeding, 2006;ChemBioChem, 7, 257 – 267.

 

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More Applications

Objective Application
Reveal the nature of protein folding variations
Mutation vs. change in folding conformation
Antibody (Rituximab) of CD20 fingerprint
Antibody optimization by fingerprint
Design peptide for a specific folding conformation
Comparison of protein conformations
Expose similarity and dissimilarity for conformers
Comparison between Insulin Receptor and IGF-1 Receptor
Misfolding in Amyloid Beta-42
Similarity score for conformation search
ATP Binding Sites on Kinases
Predict multiple protein targets for drug

 

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