Amyloid beta

IntroductionIntroduction

Alzheimer's disease is characterized by extracellular proteic plaques and intracellular neurofibrillary tangles.^[1] These plaques are collections of fibrils consisting mostly of beta-amyloid fibrils. These fibril may be aggregates of beta-sheets though it is also possible that the alpha helix forms pores in the membrane that trigger cell death.^[1] Amyloids are insoluble fibrous proteins

The most reasonable structure determined structure consists of ; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a (residues 26 and 27).^[1]

ReferencesReferences

↑ ^1.0 ^1.1 ^1.2 Crescenzi O, Tomaselli S, Guerrini R, Salvadori S, D'Ursi AM, Temussi PA, Picone D. Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. Eur J Biochem. 2002 Nov;269(22):5642-8. PMID:12423364

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Laura Olney, Michal Harel, Alexander Berchansky

[structure-1] 1.0 ^1.1 ^1.2 Crescenzi O, Tomaselli S, Guerrini R, Salvadori S, D'Ursi AM, Temussi PA, Picone D. Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. Eur J Biochem. 2002 Nov;269(22):5642-8. PMID:12423364

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