scholarly journals Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly

FEBS Letters ◽  
2012 ◽  
Vol 586 (22) ◽  
pp. 3991-3995 ◽  
Author(s):  
Axel Abelein ◽  
Lisa Lang ◽  
Christofer Lendel ◽  
Astrid Gräslund ◽  
Jens Danielsson
Keyword(s):  
Small Molecule ◽  
Self Assembly ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Molecule Interactions

Corrigendum to “Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly” [FEBS Lett. 586 (2012) 3991-3995]

FEBS Letters ◽  
2013 ◽  
Vol 587 (9) ◽  
pp. 1452-1452
Author(s):  
Axel Abelein ◽  
Lisa Lang ◽  
Christofer Lendel ◽  
Astrid Gräslund ◽  
Jens Danielsson
Keyword(s):  
Small Molecule ◽  
Self Assembly ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Molecule Interactions

Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination

2020 ◽  
Vol 32 (4) ◽  
pp. 247-255 ◽  
Author(s):  
Daniele Maiolo ◽  
Andrea Pizzi ◽  
Alessandro Gori ◽  
Greta Bergamaschi ◽  
Claudia Pigliacelli ◽  
...  
Keyword(s):  
Self Assembly ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

2013 ◽  
Vol 450 (1) ◽  
pp. 189-197 ◽  
Author(s):  
Kristoffer Brännström ◽  
Anders Öhman ◽  
Malin Lindhagen-Persson ◽  
Anders Olofsson
Keyword(s):  
Self Assembly ◽  
Molecular Mechanisms ◽  
Amyloid Β ◽  
Mechanistic Explanation ◽  
Elongation Rate ◽  
Polymerization Rate ◽  
Amyloid Β Peptide ◽  
Aβ Amyloid ◽  
Ad Alzheimer’S Disease

Identifying factors that affect the self-assembly of Aβ (amyloid-β peptide) is of utmost importance in the quest to understand the molecular mechanisms causing AD (Alzheimer's disease). Ca2+ has previously been shown to accelerate both Aβ fibril nucleation and maturation, and dysregulated Ca2+ homoeostasis frequently correlates with development of AD. The mechanisms regarding Ca2+ binding, as well as its effect on fibril kinetics, are not fully understood. Using a polymerization assay we show that Ca2+ in a dynamic and reversible manner enhances both the elongation rate and fibrillar stability, where specifically the ‘dock and lock’ phase mechanism is enhanced. Through NMR analysis we found that Ca2+ affects the fibrillar architecture. In addition, and unexpectedly, we found that Ca2+ does not bind the free Aβ monomer. This implies that Ca2+ binding requires an architecture adopted by assembled peptides, and consequently is mediated through intermolecular interactions between adjacent peptides. This gives a mechanistic explanation to the enhancing effect on fibril maturation and indicates structural similarities between prefibrillar structures and mature amyloid. Taken together we show how Ca2+ levels affect the delicate equilibrium between the monomeric and assembled Aβ and how fluctuations in vivo may contribute to development and progression of the disease.

Role of Metal Ions in the Self-assembly of the Alzheimer’s Amyloid-β Peptide

2013 ◽  
Vol 52 (21) ◽  
pp. 12193-12206 ◽  
Author(s):  
Peter Faller ◽  
Christelle Hureau ◽  
Olivia Berthoumieu
Keyword(s):  
Metal Ions ◽  
Self Assembly ◽  
Amyloid Β ◽  
The Self ◽  
Amyloid Β Peptide

scholarly journals Small Molecule Amyloid-β Protein Precursor Processing Modulators Lower Amyloid-β Peptide Levels via cKit Signaling

2019 ◽  
Vol 67 (3) ◽  
pp. 1089-1106 ◽  
Author(s):  
Ci-Di Chen ◽  
Ella Zeldich ◽  
Christina Khodr ◽  
Kaddy Camara ◽  
Tze Yu Tung ◽  
...  
Keyword(s):  
Small Molecule ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Precursor Processing ◽  
Β Protein
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