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Apolipoproteins and amyloid fibril formation in atherosclerosis

Protein & Cell 2011年第2期2卷 116-127页

作者： Chai Lean Teoh Michael D.W.Griffin Geoffrey J.Howlett Department of Biochemistry and Molecular Biology University of MelbourneParkvilleVictoria 3010Australia Bio21 Molecular Science and Biotechnology InstituteUniversity of MelbourneParkvilleVictoria 3010Australia

amyloid fibrils arise from the aggregation of misfolded proteins into highly-ordered *** accumulation of these fibrils along with some non-fibrillar constituents within amyloid plaques is associated with the pathogenesis of several human degenerative diseases.A number of plasma apolipoproteins,including apolipoprotein(apo)A-I,apoA-II,apoC-II and apoE are implicated in amyloid formation or influence amyloid formation by other *** review present knowledge of amyloid formation by apolipoproteins in disease,with particular focus on *** insights into the molecular mechanisms underlying their amyloidogenic propensity are obtained from in vitro studies which describe factors affecting apolipoprotein amyloid fibril formation and ***,we outline the evidence that amyloid fibril formation by apolipoproteins might play a role in the development and progression of atherosclerosis,and highlight possible molecular mechanisms that could contribute to the pathogenesis of this disease.

关键词： misfolding apolipoproteins amyloid fibril atherosclerosis

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Cellular and animal models to investigate pathogenesis of amyloid aggregation in neurodegenerative diseases

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Biophysics Reports 2022年第1期8卷 14-28页

作者： Houfang Long Shuyi Zeng Dan Li Interdisciplinary Research Center on Biology and Chemistry Shanghai Institute of Organic Chemistry Chinese Academy of Sciences University of Chinese Academy of Sciences Bio-X Institutes Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders Ministry of Education Shanghai Jiao Tong University Bio-X-Renji Hospital Research Center Renji Hospital School of Medicine Shanghai Jiao Tong University Zhangjiang Institute for Advanced Study Shanghai Jiao Tong University

Abnormal aggregation of amyloid proteins, e.g. amyloid β(Aβ), Tau and α-synuclein(α-syn), is closely associated with a variety of neurodegenerative diseases such as Alzheimer’s disease(AD) and Parkinson’s disease(PD). Cellular and animal models are useful to explore the neuropathology of amyloid aggregates in disease initiation and progression. In this protocol, we describe detailed procedures for how to establish neuronal and PD mouse models to evaluate amyloid pathologies including selfpropagation, cell-to-cell transmission, neurotoxicity, and impact on mouse motor and cognitive functions. We use α-syn, a key pathogenic protein in PD, as an example to demonstrate the application of the protocol, while it can be used to investigate the pathologies of other amyloid proteins as well. The established disease models are also useful to assess the activities of drug candidates for therapeutics of neurodegenerative diseases.

关键词： amyloid fibril Primary neuron Mouse model Parkinson’s disease α-Synuclein

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The Effect of Heme on the Thermal Stability of Myoglobin under Conditions of amyloidsis

The Effect of Heme on the Thermal Stability of Myoglobin und...

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第二届全国“跨学科蛋白质研究”学术讨论会

作者：李正强 Key Laboratory for Molecular Enzymology&Engineering the Ministry of Education(Jilin University)Changchun 130021China

Prosthetic group affects the holoprotein stability and the passway of protein folding/*** find the heme effect under the condition of ***,DSC,ATR-FTIR,CD and ThT fluorescence assay have been adopted to study the kinetics of amyloidsis of apomyoglobin as well as myoglobin,especially in the early stage (the first 120min).The results show that heme has

关键词： apomyoglobin myoglobin prothetic group heme amyloid fibril DSC ATR-IR CD ThT.

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Investigation of the interactions between the aptamer and Aβ species by single molecule force spectroscopy

Investigation of the interactions between the aptamer and A...

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第十届全国化学生物学学术会议

作者： Yan Zheng Zhiping Li Qing Wang Xiaohai Yang Kemin Wang Wenyan Nie Xiuhua Geng Xiaofeng Liu Liyuan Zou State Key Laboratory of Chemo/Biosensing and Chemometrics College of Chemistry and Chemical EngineeringKey Laboratory for Bio-Nanotechnology and Molecular Engineering of Hunan ProvinceHunan University

Increasing knowledge on the understanding interactions of aptamer with misfolded proteins（including monomer, oligomer and amyloid fibril） is crucial for diagnosis of amyloid diseases. Herein, the interactions of aptamer with amyloid β（Aβ） monomer, Aβ oligomer and Aβ fibril were investigated using single molecule force spectroscopy（SMFS）. The results revealed that the aptamer screened against Aβ oligomer could not bind to Aβ monomer, while it could bind to Aβ oligomer and Aβ fibril. An intersting discovery was that the binding force distribution of the aptamer with Aβ oligomer displayed unimodal distribution, while it displayed bimodal distribution for the aptamer with Aβ fibril. The phenomena may be attributed to the inherent structural differences of Aβ species, the flexible conformation of aptamer and the change of electrostatic interaction. This work demonstrated that SMFS could be a powerful tool to clearly distinguish Aβ monomer, Aβ oligomer and Aβ fibril. Moreover, the binding behaviour of the aptamer with Aβ species at single molecule level also provided abundant information for comprehensive applications of aptamer probes in diagnosis of Alzheimer’s.

关键词： Aptamer Monomer Oligomer amyloid fibril Single molecule force spectroscopy

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人类微球蛋白氨基酸片段的全原子分子动力学模拟蛋白质聚集分子机制研究

人类微球蛋白氨基酸片段的全原子分子动力学模拟蛋白质聚集分子机...

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作者：梁崇文复旦大学

学位级别：硕士

The human neurodegenerative diseases and amyloidosis have aroused public attention in the past few years,and it is supposed that these kinds of disease connect with protein misfolding and ***,their mechanism and process are not so clear revealed by scientific reports so *** so-called "amyliodosis" are the series of diseases,including Alzheimer's disease, Parkinson's disease,Huntington's disease,prion disease,Down Syndrom,multiple Myeloma and Chronic Renal Failure *** tissue samples of these diseases share the same features under the observation of microscopy,and we can see amyloid fibrils withβ-sheet zipper ***,the native states of these proteins are soluble in physiological condition,however,the misfolded proteins aggregate to the insoluble amyloid fibrils and cannot be decomposed by enzymes.The humanβ2-microglobulin was verified as a key role of dialysis related *** amyioid fibrils aggregated by insoluble denatured protein damage human tissues and then cause the renal failure and bone/joint *** of humanβ2-microglobulin is a severe complication always found in patients who receive long time hemo-dialysis.In recent years,many reports show that two fragments 20-41 and 83-99 in humanβ2-microglobulin play important roles in protein aggregation and amyloid *** et *** that the fragments 72-99,83-89 and 91-96 can form amyloid fibrils by themselves in ***,they predict that the fragment 83-99 form a typicalβ-hairpin structure to stack and construct of the spine region of amyloid *** et *** that the K3 peptide can form amyloid fibrils by itself in several different solvent conditions,and use solid state NMR to reveal the 3D structure of K3 *** propose that the fibril state K3 peptide is with trans Pro32 and the region 20-28 flips over by comparing with native state,the hydrophobic side-chain of Phe22 and Tyr26 are buried inside the double laye

关键词： Humanβ2-microglobulin Protein aggregation amyloid fibril All-atom Molecular dynamics Replica Exchange Method GROMACS Free energy landscape

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Solid-state NMR reveals the structural transformation of the TDP-43 amyloidogenic region upon fibrillation

Solid-state NMR reveals the structural transformation of the...

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2021年全国生物相分离和相变学术研讨会

作者： Jun-xia Lu Xiao-feng Zhuo School of Life Science and Technology Shanghai Tech University

TDP-43 is a primary pathological hallmark protein of amyotrophic lateral sclerosis and frontotemporal lobar degeneration,which may exist in the form of amyloid inclusions in the cells of *** addition to serving as a biomarker for these diseases,TDP-43 can also directly trigger *** previously determined the amyloidogenic core region of TDP-43(residues 311-360) and showed by solution NMR that this region includes two α-helices [(321-330) and(335-343)] in *** suggested that the helix-to-sheet structural transformation initiates TDP-43 *** the present study,X-ray diffraction shows that TDP-43(311-360) aggregates adopt a cross-β ***(Trx) fused TDP-43(311-360) can undergo liquid-liquid phase separation(LLPS) before fibrillation,suggesting that phase separation is an intermediate step before amyloid ***-state NMR(SSNMR),carried out to elucidate the structural changes of TDP-43(311-360) at the atomic level,indicates five β-strands of the amyloids formed,with the major two β-strands contributed by the first helical region in the solution *** NMR evidence is also in support of the fibril having a parallel in-register conformation,implying a mechanism in which the helix-helix interactions in LLPS are converted into β-strand parallel lateral association upon *** studies have assigned many key inter-residue interactions that contribute to the stability of the fibril,including F316 with 1318 and Q327 and W334 with A325,A326,A329 and *** with H-detection reveals a unique close interaction between the indole Nε1-Hε1 of W334 and the side-chain carbonyl of *** interaction could be a very important factor in initiating TDP-43(311-360) folding/misfolding in LLPS.

关键词： TDP-43(311-360) TDP-16(267-414) Liquid-liquid phase separation amyloid fibril solid-state NMR

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