Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation

2021 ◽  
Author(s):  
Joana S. Cristóvão ◽  
Guilherme G. Moreira ◽  
Filipe E. P. Rodrigues ◽  
Ana P. Carapeto ◽  
Mário S. Rodrigues ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Chaperone Activity ◽  
Amyloid Aggregation ◽  
Chemical Regulation ◽  
Aggregation Activity

A mechanism of chemical regulation of the S100B chaperone via Cu2+ induced assembly of S100B cross-linked oligomers with enhanced anti-amyloid aggregation activity.

scholarly journals Link between Diabetes and Alzheimer’s Disease Due to the Shared Amyloid Aggregation and Deposition Involving Both Neurodegenerative Changes and Neurovascular Damages

2020 ◽  
Vol 9 (6) ◽  
pp. 1713 ◽  
Author(s):  
Gabriela Dumitrita Stanciu ◽  
Veronica Bild ◽  
Daniela Carmen Ababei ◽  
Razvan Nicolae Rusu ◽  
Alina Cobzaru ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Social Impact ◽  
Significant Risk ◽  
Amyloid Β ◽  
Detailed Knowledge ◽  
Amyloid Aggregation ◽  
Islet Amyloid ◽  
Type 3 ◽  
Insight Into

Diabetes and Alzheimer’s disease are two highly prevalent diseases among the aging population and have become major public health concerns in the 21st century, with a significant risk to each other. Both of these diseases are increasingly recognized to be multifactorial conditions. The terms “diabetes type 3” or “brain diabetes” have been proposed in recent years to provide a complete view of the potential common pathogenic mechanisms between these diseases. While insulin resistance or deficiency remains the salient hallmarks of diabetes, cognitive decline and non-cognitive abnormalities such as impairments in visuospatial function, attention, cognitive flexibility, and psychomotor speed are also present. Furthermore, amyloid aggregation and deposition may also be drivers for diabetes pathology. Here, we offer a brief appraisal of social impact and economic burden of these chronic diseases and provide insight into amyloidogenesis through considering recent advances of amyloid-β aggregates on diabetes pathology and islet amyloid polypeptide on Alzheimer’s disease. Exploring the detailed knowledge of molecular interaction between these two amyloidogenic proteins opens new opportunities for therapies and biomarker development.

pH-mediated control of anti-aggregation activities of cyanobacterial and E. coli chaperonin GroELs

2020 ◽  
Author(s):  
Tahmina Akter ◽  
Hitoshi Nakamoto
Keyword(s):  
Escherichia Coli ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Ph Dependence ◽  
Chaperone Activity ◽  
Ph Change ◽  
Aggregation Assay ◽  
E Coli ◽  
Aggregation Activity

Abstract In contrast to Escherichia coli, cyanobacteria have multiple GroELs, the bacterial homologues of chaperonin/Hsp60. We have shown that cyanobacterial GroELs are mutually distinct and different from E. coli GroEL with which the paradigm for chaperonin structure/function has been established. However, little is known about regulation of cyanobacterial GroELs. This study investigated effect of pH (varied from 7.0 to 8.5) on chaperone activity of GroEL1 and GroEL2 from the cyanobacterium Synechococcus elongatus PCC7942 and E. coli GroEL. GroEL1 and GroEL2 showed pH dependency in suppression of aggregation of heat-denatured malate dehydrogenase, lactate dehydrogenase and citrate synthase. They exhibited higher anti-aggregation activity at more alkaline pHs. Escherichia coli GroEL showed a similar pH-dependence in suppressing aggregation of heat-denatured lactate dehydrogenase. No pH dependence was observed in all the GroELs when urea-denatured lactate dehydrogenase was used for anti-aggregation assay, suggesting that the pH-dependence is related to some denatured structures. There was no significant influence of pH on the chaperone activity of all the GroELs to promote refolding of heat-denatured malate dehydrogenase. It is known that pH in cyanobacterial cytoplasm increases by one pH unit following a shift from darkness to light, suggesting that the pH-change modulates chaperone activity of cyanobacterial GroEL1 and GroEL2.

The Alzheimer’s therapeutic PBT2 promotes amyloid-β degradation and GSK3 phosphorylation via a metal chaperone activity

2011 ◽  
Vol 119 (1) ◽  
pp. 220-230 ◽  
Author(s):  
Peter J. Crouch ◽  
Maria S. Savva ◽  
Lin W. Hung ◽  
Paul S. Donnelly ◽  
Alexandra I. Mot ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Chaperone Activity

scholarly journals Real-time monitoring of the aggregation of Alzheimer's amyloid-β via1H magic angle spinning NMR spectroscopy

2018 ◽  
Vol 54 (16) ◽  
pp. 2000-2003 ◽  
Author(s):  
Jian Wang ◽  
Tomoya Yamamoto ◽  
Jia Bai ◽  
Sarah J. Cox ◽  
Kyle J. Korshavn ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Real Time ◽  
Amyloid Β ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Amyloid Aggregation ◽  
Real Time Monitoring ◽  
Angle Spinning ◽  
Mechanical Rotation

Magic-angle-spinning NMR for monitoring amyloid aggregation reveals that mechanical rotation of Aβ1–40 monomers increases the rate of aggregation.

Synthesis of derivatives of cleistopholine and their anti-acetylcholinesterase and anti-β-amyloid aggregation activity

2018 ◽  
Vol 76 ◽  
pp. 228-236 ◽  
Author(s):  
Zhenhua Wu ◽  
Wenxia Liao ◽  
Kelin Chen ◽  
Jingfang Qin ◽  
Huang Tang
Keyword(s):  
Amyloid Aggregation ◽  
Β Amyloid ◽  
Aggregation Activity ◽  
Derivatives Of

Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties

2017 ◽  
Vol 13 (8) ◽  
pp. 1545-1551 ◽  
Author(s):  
Elaheh Jamasbi ◽  
Frances Separovic ◽  
Mohammed Akhter Hossain ◽  
Giuseppe Donato Ciccotosto
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Amyloid Plaques ◽  
Full Length ◽  
Amyloid Β Peptide ◽  
Amyloid Aggregation ◽  
Cell Binding ◽  
The Brain

Phosphorylation of Aβ42 promotes the formation of amyloid plaques in the brain, which lack the neurotoxic properties associated with oligomeric species causing pathogenesis in Alzheimer's disease.

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.

Anti-β-amyloid aggregation activity of enantiomeric furolactone-type lignans from Archidendron clypearia (Jack) I.C.N.

2018 ◽  
Vol 34 (4) ◽  
pp. 456-463 ◽  
Author(s):  
Yu-Xi Wang ◽  
Bin Lin ◽  
Le Zhou ◽  
Zhi-Yang Yan ◽  
Han Zhang ◽  
...  
Keyword(s):  
Amyloid Aggregation ◽  
Β Amyloid ◽  
Aggregation Activity

scholarly journals The Binding of Apolipoprotein E to Oligomers and Fibrils of Amyloid-β Alters the Kinetics of Amyloid Aggregation

Biochemistry ◽  
2014 ◽  
Vol 53 (40) ◽  
pp. 6323-6331 ◽  
Author(s):  
Kanchan Garai ◽  
Philip B. Verghese ◽  
Berevan Baban ◽  
David M. Holtzman ◽  
Carl Frieden
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Aggregation ◽  
Kinetics Of
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