Specific Binding of a β-Cyclodextrin Dimer to the Amyloid β Peptide Modulates the Peptide Aggregation Process

Biochemistry ◽  
2012 ◽  
Vol 51 (21) ◽  
pp. 4280-4289 ◽  
Author(s):  
Anna Wahlström ◽  
Risto Cukalevski ◽  
Jens Danielsson ◽  
Jüri Jarvet ◽  
Hideki Onagi ◽  
...  
Keyword(s):  
Specific Binding ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation ◽  
Aggregation Process ◽  
Cyclodextrin Dimer

scholarly journals β-Hairpin mimics containing a piperidine–pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species

2017 ◽  
Vol 8 (2) ◽  
pp. 1295-1302 ◽  
Author(s):  
S. Pellegrino ◽  
N. Tonali ◽  
E. Erba ◽  
J. Kaffy ◽  
M. Taverna ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation ◽  
Aggregation Process ◽  
Amyloid Aggregation ◽  
Protein Protein Interactions ◽  
Β Amyloid

Acyclic β-hairpins designed on oligomeric and fibril structures of Aβ1–42 disrupt protein–protein interactions mediating amyloid β-peptide aggregation.

The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

2017 ◽  
Vol 229 ◽  
pp. 110-114 ◽  
Author(s):  
F. Stellato ◽  
Z. Fusco ◽  
R. Chiaraluce ◽  
V. Consalvi ◽  
S. Dinarelli ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation ◽  
Aggregation Process ◽  
Β Sheet

Modulation of amyloid β peptide aggregation by hydrophilic polymers

2019 ◽  
Vol 21 (37) ◽  
pp. 20999-21006
Author(s):  
Zhanna Evgrafova ◽  
Bruno Voigt ◽  
Andreas H. Roos ◽  
Gerd Hause ◽  
Dariush Hinderberger ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Hydrophilic Polymers ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation ◽  
Amyloidogenic Protein

Careful balance of hydrophilicity of precisely engineered polymers alters aggregation of the amyloidogenic protein Aβ1–40.

Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptides

2000 ◽  
Vol 349 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Marc H. BAUMANN ◽  
Jukka KALLIJÄRVI ◽  
Hilkka LANKINEN ◽  
Claudio SOTO ◽  
Matti HALTIA
Keyword(s):  
Apolipoprotein E ◽  
Binding Site ◽  
Late Onset ◽  
Specific Binding ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Structural Motif ◽  
Amyloid Β Peptide ◽  
High Avidity ◽  
Amyloidogenic Protein

Inheritance of the apolipoprotein E (apoE) ϵ4 allele is a risk factor for late-onset Alzheimer's disease (AD). Biochemically apoE is present in AD plaques and neurofibrillary tangles of the AD brain. There is a high avidity and specific binding of apoE and the amyloid β-peptide (Aβ). In addition to AD apoE is also present in many other cerebral and systemic amyloidoses, Down's syndrome and prion diseases but the pathophysiological basis for its presence is still unknown. In the present study we have compared the interaction of apoE with Aβ, the gelsolin-derived amyloid fragment AGel183-210 and the amyloidogenic prion fragments PrP109-122 and PrP109-141. We show that, similar to Aβ, also AGel and PrP fragments can form a complex with apoE, and that the interaction between apoE and the amyloidogenic protein fragments is mediated through the same binding site on apoE. We also show that apoE increases the thioflavin-T fluorescence of PrP and AGel and that apoE influences the content of β-sheet conformation of these amyloidogenic fragments. Our results indicate that amyloids and amyloidogenic prion fragments share a similar structural motif, which is recognized by apoE, possibly through a single binding site, and that this motif is also responsible for the amyloidogenicity of these fragments.

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