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Molecular dynamics studies of the inhibitory mechanism of copper(Ⅱ) on aggregation of amyloid β-peptide

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Chinese Chemical Letters 2007年第3期18卷 357-360页

作者： Yong Jiao Pin Yang Institute of Molecular Science Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education Shanxi University Taiyuan 030006 China

The inhibitory mechanism of copper（Ⅱ） on the aggegation of amyloid β-peptide （Aβ） was investigated by molecular dynamics simulations. The binding mode ofcopper（Ⅱ） with Aβ is characterized by the imidazole nitrogen atom, Nπ, of the histidine residue H 13, acting as the anchoring site, and the backbone＇s deprotoned amide nitogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils.

关键词： Copper(Ⅱ) amyloid β-peptide Inhibitory mechanism Alzheimer's disease Molecular dynamics Radial distribution function (RDF)

维普期刊数据库

Cu（Ⅱ） attenuates oligomeic and fibrillar A β-induced activation of BV-2 microglia cells

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Cu（Ⅱ） attenuates oligomeic and fibrillar A β-induced act...

Regulation of amyloid β-peptid eproduction by G protein-coupled receptors

中国神经科学学会第四次会员代表大会暨第八届全国学术会议

作者： Han-Chang HANG~(1 *) Xue-Ling DAI~1 Xiao-Hui YANG~2 Wei XU~1 Lin CHEN~2 Zhao-Feng JIANG~(1 *) 1 College of Arts and Sciences Beijing Union University Beijing 100191 China 2 College of Life Science Capital Normal University Beijing 100037 China

＜正＞Background amyloid-β peptide（Aβ） is one of the main components of senile plaques,a pathological hallmark of Alzheimer’s disease（AD）.Activated microglia represents a major source of inflammatory factors in Alzheimer’s disease and a possible source of cytotoxic factors.Aβpeptide has been shown to activate microglia and stimulate their production of inflammatory *** evidence has shown that the redox-active biometal Cu（Ⅱ） can modulate the physiochemical properties of Aβ.This article aims to evaluate the effect of oligomeric and fibrillar Aβand Cu（Ⅱ） on microglia activation. Methods Oligomeric and fibrilliar Aβwere prepared by incubation at 4℃for 24h or at 37℃for 7days,respectively.Aβpeptide assemblies were extensively characterized by CD,TH-T fluorescence and sedimentation *** the Aβ-Cu（Ⅱ） complex preparation,the above oligomeric and fibrillar Aβwere incubated with Cu（Ⅱ） for 1h to form the Aβ-Cu（Ⅱ） complexes, *** immortalized murine BV-2 cells were grown and maintained in Dulbecco’s Modified Eagles Medium （DMEM）（supplemented with 10%fetal bovine serum and 100 mg/mL streptomycin and 10 U/mL penicillin） at 37℃in a humidified incubator with 5%CO2.20μM concentration of oligomeric or fillbrillar Aβwas chosen,and LPS was chosen as positive control and PBS as vehicle *** viability was quantitively determined using the MTT *** BV-2 cells co-incubated with different forms of Aβor their Aβ-Cu（Ⅱ） complexes for 24 h,real-time PCR（RT-PCR） detected TNFαand iNOS mRNA expression levels of BV-2 *** production of nitric oxide（NO） was quantified by measuring the released NO metabolites（nitrate and nitrite） with Griess *** Cu（Ⅱ） has an important effect on the oligomeric and filbrillar Aβsecondary structure and aggregation,and will disrupts p-sheet structure and convertsβaggregates into non-β*** oligomeric and filbrillar Aβcan induce microglial activation,however the cellular signal ways are different due to t

关键词： Alzheimer’s disease amyloid β-peptide copper nitric oxide(NO) TNFβ

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Regulation of amyloid β-peptid eproduction by G protein-cou...

Oligomeric and fibrillar species of β-amyloid(Aβ42) both impair mitochondrial function in P301L tau transgenic mice

中国神经科学学会第六届学术会议暨学会成立十周年庆祝大会

作者： Ni Yan-xiang , Zhao Xiao-hui , Bao Guo-bin, Zou Lin, Wang Zhu, Teng Lin, Guo Ming, Pei Gang Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences Graduate School of the Chinese Academy of Sciences, Shanghai 200031, China

＜正＞Accumulation of amyloid β-peptide （Aβ）. is a hallmark and primary cause of Alzheimer disease （AD）. Mutation can affect the activity of γ-secretase, a pivotal enzyme for Aβproduction and AD pathogenesis. However, it is largely unknown whether and how γ-secretase activity and Aβproduction a re regulated by physiological signals, many of which are mediated by G protein-coupled receptors （GPCRs）. Here we report that stimulation of β2-adrenergic receptors or δ-opioid receptors in hippocampal cells in vitro or in vivo enhances γ-secretase activity, resulting in increased Aβproduction. This enhancement requires agonist-induced endocytosis of these receptors and trafficking of γ-secretase to late endosomes and lysosomes, where Aβproduction is elevated. Thus, physiological signals can regulate Aβproduction and aberration of this regulation may contribute to AD pathogenesis.

关键词： G protein-coupled receptor amyloid β-peptide regulation Alzheimer disease

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世界最新医学信息文摘 2016年第4期 8-8页

作者： Anne Eckert Susanne Hauptmann Isabel Scherping Jessica Meinhardt Virginie Rhein Stefan Drse Ulrich Brandt Marcus Fndrich Walter E.Müller Jiirgen Gtz

We recently provided evidence for a mitochondrial dysfunction in P301L tau transgenic mice,a strain modeling the tau pathology of Alzheimer's disease(AD)and frontotemporal dementia(FTD).In addition to tau aggregates,the AD brain is further characterized by Aβpeptide-containing *** we addressed the role of Aβ,this indicated a synergistic action of tau and Aβpathology on the *** the present study,we compared the toxicity of different Aβ42 conformations in light of recent studies suggesting that oligomeric rather than fibrillar Aβmight be the actual toxic ***,both oligomeric and fibrillar,but not disaggregated(mainly monomeric)Aβ42 caused a decreased mitochondrial membrane potential in cortical brain cells obtained from FTD P301L tau transgenic *** was not observed with cerebellar preparations indicating selective vulnerability of cortical ***,we found reductions in state 3 respiration,the respiratory control ratio,and uncoupled respiration when incubating P301L tau mitochondria either with oligomeric or fibrillar preparations of Aβ***,we found that aging specifically increased the sensitivity of mitochondria to oligomeric Aβ42 damage indicating that oligomeric and fibrillar Aβ42 are both toxic,but exert different degrees of toxicity.

关键词： Alzheimer’s disease amyloid aggregates amyloid β-peptide amyloid toxicity Fibrils Frontotemporal dementia Globulomer Mitochondria Oligomer Protein aggregation Respiration Tau Transgenic mice

Oligomeric and fibrillar species of β-amyloid(A β 42) both impair mitochondrial function in P301L tau transgenic mice

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世界最新医学信息文摘 2015年第99期 1-1页

作者： Anne Eckert Susanne Hauptmann Isabel Scherping Jessica Meinhardt Virginie Rhein Stefan Dr?se Ulrich Brandt Marcus F?ndrich Walter E.Müller Jürgen G?tz

We recently provided evidence for a mitochondrial dysfunction in P301L tau transgenic mice, a strain modeling the tau pathology of alzheimer's disease(ad) and frontotemporal dementia(ftd). in addition to tau aggregates, the ad brain is further characterized by Aβ peptide-containing plaques. When we addressed the role of Aβ, this indicated a synergistic action of tau and Aβ pathology on the mitochondria. In the present study, we compared the toxicity of different Aβ42 conformations in light of recent studies suggesting that oligomeric rather than fibrillar Aβ might be the actual toxic species. Interestingly, both oligomeric and fibrillar, but not disaggregated(mainly monomeric) Aβ42 caused a decreased mitochondrial membrane potential in cortical brain cells obtained from FTD P301L tau transgenic mice. This was not observed with cerebellar preparations indicating selective vulnerability of cortical neurons. Furthermore, we found reductions in state 3 respiration, the respiratory control ratio, and uncoupled respiration when incubating P301L tau mitochondria either with oligomeric or fibrillar preparations of Aβ42. Finally, we found that aging specifically increased the sensitivity of mitochondria to oligomeric Aβ42 damage indicating that oligomeric and fibrillar Aβ42 are both toxic, but exert different degrees of toxicity.

关键词： Alzheimer’s disease amyloid aggregates amyloid β-peptide amyloid toxicity Fibrils Frontotemporal dementia Globulomer Mitochondria oligomer Protein aggregation respiration tau transgenic mice

Oligomeric and fibrillar species of β-amyloid(Aβ42) both impair mitochondrial function in P301L tau transgenic mice

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世界最新医学信息文摘 2015年第A期 8-8页

作者： Anne Eckert Susanne Hauptmann Isabel Scherping Jessica Meinhardt Virginie Rhein Stefan Dr?se Ulrich Brandt Marcus F?ndrich Walter E.Müller Jürgen G?tz

We recently provided evidence for a mitochondrial dysfunction in P301 l tau transgenic mice, a strain modeling the tau pathology of alzheimer's disease(ad) and frontotemporal dementia(ftd). in addition to tau aggregates, the ad brain is further characterized by Aβ peptide-containing plaques. When we addressed the role of Aβ, this indicated a synergistic action of tau and Aβ pathology on the mitochondria. In the present study, we compared the toxicity of different Aβ42 conformations in light of recent studies suggesting that oligomeric rather than fibrillar Aβ might be the actual toxic species. Interestingly, both oligomeric and fibrillar, but not disaggregated(mainly monomeric) Aβ42 caused a decreased mitochondrial membrane potential in cortical brain cells obtained from FTD P301 L tau transgenic mice. This was not observed with cerebellar preparations indicating selective vulnerability of cortical neurons. Furthermore, we found reductions in state 3 respiration, the respiratory control ratio, and uncoupled respiration when incubating P301 L tau mitochondria either with oligomeric or fibrillar preparations of Aβ42. Finally, we found that aging specifically increased the sensitivity of mitochondria to oligomeric Aβ42 damage indicating that oligomeric and fibrillar Aβ42 are both toxic, but exert different degrees of toxicity.