l-Ala Modified Analogues of Amyloid β-Peptide Residue 17-20: Self-Association and Amyloid-like Fibril Formation

2006 ◽  
Vol 12 (4) ◽  
pp. 341-348 ◽  
Author(s):  
Debasish Haldar ◽  
Arindam Banerjee
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide ◽  
Peptide Residue ◽  
Self Association

Sodium-salt adduct fullerenes prevent self-association and amyloid β fibril formation: molecular dynamics approach

2020 ◽  
Vol 18 (2-3) ◽  
pp. 335-347
Author(s):  
Miguel Angel Balderas Altamirano ◽  
Gustavo Basurto-Islas ◽  
Melchor Martínez-Herrera ◽  
Juan Luis Pichardo Molina ◽  
Susana Figueroa-Gerstenmaier
Keyword(s):  
Molecular Dynamics ◽  
Sodium Salt ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Self Association

A sulfated proteoglycan aggregation factor mediates amyloid-β peptide fibril formation and neurotoxicity

Amyloid ◽  
1999 ◽  
Vol 6 (4) ◽  
pp. 233-243 ◽  
Author(s):  
Joanne McLaurin ◽  
Trudy Franklin ◽  
William J Kuhns ◽  
Paul E. Fraser
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide ◽  
Aggregation Factor

A Mobile Precursor Determines Amyloid-β Peptide Fibril Formation at Interfaces

2012 ◽  
Vol 134 (34) ◽  
pp. 14172-14178 ◽  
Author(s):  
Lei Shen ◽  
Takuji Adachi ◽  
David Vanden Bout ◽  
X.-Y. Zhu
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide

A Disulfide-Linked Amyloid-β Peptide Dimer Forms a Protofibril-like Oligomer through a Distinct Pathway from Amyloid Fibril Formation

Biochemistry ◽  
2010 ◽  
Vol 49 (33) ◽  
pp. 7100-7107 ◽  
Author(s):  
Takahiro Yamaguchi ◽  
Hisashi Yagi ◽  
Yuji Goto ◽  
Katsumi Matsuzaki ◽  
Masaru Hoshino
Keyword(s):  
Amyloid Fibril ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide ◽  
Amyloid Fibril Formation

A Structural Motif of Acetylcholinesterase That Promotes Amyloid β-Peptide Fibril Formation†

Biochemistry ◽  
2001 ◽  
Vol 40 (35) ◽  
pp. 10447-10457 ◽  
Author(s):  
Giancarlo V. De Ferrari ◽  
Mauricio A. Canales ◽  
Irina Shin ◽  
Lev M. Weiner ◽  
Israel Silman ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Structural Motif ◽  
Amyloid Β Peptide

A carboxylated Zn-phthalocyanine inhibits fibril formation of Alzheimer's amyloid β peptide

FEBS Journal ◽  
2014 ◽  
Vol 282 (3) ◽  
pp. 463-476 ◽  
Author(s):  
Shatera Tabassum ◽  
Abdullah M. Sheikh ◽  
Shozo Yano ◽  
Takafumi Ikeue ◽  
Makoto Handa ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide

Inhibition of Aβ(1–40) fibril formation by cyclophilins

2016 ◽  
Vol 473 (10) ◽  
pp. 1355-1368 ◽  
Author(s):  
Marten Villmow ◽  
Monika Baumann ◽  
Miroslav Malesevic ◽  
Rolf Sachs ◽  
Gerd Hause ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Water Soluble ◽  
Main Process ◽  
Amyloid Β Peptide ◽  
Cyclophilin D ◽  
Aβ Amyloid

Cyclophilins interact directly with the Alzheimer's disease peptide Aβ (amyloid β-peptide) and are therefore involved in the early stages of Alzheimer's disease. Aβ binding to CypD (cyclophilin D) induces dysfunction of human mitochondria. We found that both CypD and CypA suppress in vitro fibril formation of Aβ(1–40) at substoichiometric concentrations when present early in the aggregation process. The prototypic inhibitor CsA (cyclosporin A) of both cyclophilins as well as the new water-soluble MM258 derivative prevented this suppression. A SPOT peptide array approach and NMR titration experiments confirmed binding of Aβ(1–40) to the catalytic site of CypD mainly via residues Lys16–Glu22. The peptide Aβ(16–20) representing this section showed submicromolar IC50 values for the peptidyl prolyl cis–trans isomerase activity of CypD and CypA and low-micromolar KD values in ITC experiments. Chemical cross-linking and NMR-detected hydrogen–deuterium exchange experiments revealed a shift in the populations of small Aβ(1–40) oligomers towards the monomeric species, which we investigated in the present study as being the main process of prevention of Aβ fibril formation by cyclophilins.

Sign in / Sign up

Export Citation Format

Share Document