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P3 peptide : ウィキペディア英語版
P3 peptide

p3 peptide also known as amyloid β- peptide (Aβ)17–40/42 is the peptide resulting from the α- and γ-secretase cleavage from the amyloid precursor protein (APP). It is known to be the major constituent of diffuse plaques observed in Alzheimer's disease (AD) brains and pre-amyloid plaques in people affected of Down syndrome. However, p3 peptide's role in these diseases is not truly known yet.
== Structure ==

There is little information related to the p3 peptides composition and structure, and moreover most of it has to do with characteristics that concern to its roll in Alzheimer's disease. p3 can be found as a 24 or 26 residues peptide, depending on which is gamma secretase's cleavage. The peptide which has 26 residues, presents the following sequence:
* VFFAEDVGSNKGAIIGLMVGGVVIAT〔(【引用サイトリンク】title=Sequence Search: VFFAEDVGSNKGAIIGLMVGGVVIAT )
In relation to the secondary structure of p3 peptide, it is thought that after the cleavage by the α- and γ- secretases and extraction from the membrane it would convert quickly from the α-helix conformation it has when it is part of APPsα sequence to a β-hairpin structure. Then, this highly hydrophobic monomer would rapidly evolve into fibrils with no soluble intermediate forms, the ones related to amyloid’s structure. The main reason why p3 does not aggregate in amyloidogenic forms while does, is that the N-terminal domain1–16, which is present in Aβ’s sequence but not in p3's one, is known to protect the hydrophobic core of the oligomers from being dissolved by the watered medium. So, p3 peptide oligomers would likely expose hydrophobic residues to water and would be less stable. As a consequence, p3 peptide structural determinants can assemble into fibrils, but no oligomeric forms have been identified. That is why p3 peptide represents the benign form of amyloid.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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