共查询到20条相似文献,搜索用时 31 毫秒
1.
AD (Alzheimer’s disease) is a progressive neurodegenerative disorder characterized by the cerebral accumulation of fibrillar amyloid‐beta (Aβ) aggregates. Here we present the electrochemistry of two novel sym‐triazine derivatives (TAE‐1, TAE‐2) as modulators of Aβ1–42 aggregation in vitro. Incubation studies conducted at physiological conditions demonstrated strong inhibition of β‐sheet fibril formation. Uniquely, square‐wave voltammetry indicated progressive changes in the surface‐availability of amyloid‐intercalated triazines for oxidation, mediated by competing peptide self‐assembly. Time‐resolved voltammetric analysis showed increasing anodic peak currents (≥3‐fold) and progressive shifts in redox potentials, measured over 24 h. The more potent aggregation modulator (TAE‐2) showed prolonged association during the pre‐nucleation states of Aβ. 相似文献
2.
A Method for Evaluating the Level of Soluble β‐Amyloid(1–40/1–42) in Alzheimer’s Disease Based on the Binding of Gelsolin to β‐Amyloid Peptides
下载免费PDF全文
![点击此处可从《Angewandte Chemie (International ed. in English)》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Dr. Yanyan Yu Lin Zhang Dr. Chenglin Li Xiaoyu Sun Dr. Daoquan Tang Prof. Guoyue Shi 《Angewandte Chemie (International ed. in English)》2014,53(47):12832-12835
In the present work, a new electrochemical strategy for the sensitive and specific detection of soluble β‐amyloid Aβ(1–40/1–42) peptides in a rat model of Alzheimer’s disease (AD) is described. In contrast to previous antibody‐based methods, β‐amyloid(1–40/1–42) was quantified based on its binding to gelsolin, a secretory protein present in the cerebrospinal fluid (CSF) and plasma. The level of soluble β‐amyloid peptides in the CSF and various brain regions were found with this method to be lower in rats with AD than in normal rats. 相似文献
3.
Understanding the structure of amyloid‐β (Aβ) aggregates is a key step towards elucidating the pathology of Alzheimer’s disease. In this work, three fragments of the Aβ1–42 protein, Aβ1–25 (DAEFRHDSGYEVHHQKLVFFAEDVG), Aβ25–35 (GSNKGAIIGLM), and Aβ33–42 (GLMVGGVVIA), were synthesized, and their aggregated structures were examined by linear infrared spectroscopy in the amide‐I (mainly the C?O stretching) region. The structures of the formed aggregates were found to be both sequence and pH dependent. The results suggest that instead of forming matured fibrils, as in the case of full‐length Aβ1–42, both Aβ1–25 and Aβ33–42 form a mixture of threadlike β‐sheet fibril, soluble β‐sheet oligomer, and random coil structures. The β‐sheet conformations were found to be mainly antiparallel for the former and both parallel and antiparallel for the latter. However, the Aβ25–35 fragment was found to form assembled fibrils containing predominantly parallel β‐sheets. The conformation and morphology of the aggregates were also confirmed by circular dichroism measurements and transmission electron microscopy. Factors influencing the structures of the aggregates formed by the Aβ fragments were discussed. 相似文献
4.
Bo Pang Xiaoyu Zhuang Xinyu Bian Shu Liu Zhiqiang Liu Fengrui Song 《Journal of mass spectrometry : JMS》2020,55(10)
A wealth of epidemiological evidence indicates a strong link between type 2 diabetes (T2D) and Alzheimer's disease (AD). The fiber deposition with cross‐β‐sheet structure formed by self‐aggregation and misfolding of amyloidogenic peptides is a common hallmark of both diseases. For the patients with T2D, the fibrils are mainly found in the islets of Langerhans that results from the accumulation of human islet amyloid polypeptide (hIAPP). The major component of aggregates located in the brain of AD patients is amyloid‐β (Aβ). Many biophysical and physiological properties are shared by hIAPP and Aβ, and both peptides show similar cytotoxic mechanisms. Therefore, it is meaningful to investigate the possible cross‐interactions of hIAPP and Aβ in both diseases. In this article, the segment 25–35 of Aβ was selected because Aβ25–35 was a core region in the process of amyloid formation and showed similar aggregation tendency and toxicity with full‐length Aβ. The electrospray ionization‐ion mobility‐mass spectrometry analysis and thioflavin T fluorescence kinetic analysis combined with transmission electron microscopy were used to explore the effects of the coexistence of Aβ25–35 and hIAPP on the self‐aggregation of both peptides and whether there was co‐assembly in fibrillation. The results indicated that the aggregation of hIAPP and Aβ25–35 had two nucleation stages in the binary mixtures. hIAPP and Aβ25–35 had a high binding affinity and a series of hetero‐oligomers formed in the mixtures of hIAPP and Aβ25–35 in the early stage. The cross‐reaction between hIAPP monomers and Aβ25–35 monomers as well as a little of oligomers during primary nucleation stage could accelerate the aggregation of Aβ25–35. However, owing to the obvious difference in aggregation ability between hIAPP and Aβ25–35, this cross‐interaction had no significant impact on the self‐assembly of hIAPP. Our study may offer a better understanding for exploring the molecular mechanism of the association between AD and T2D observed in clinical and epidemiological studies and developing therapeutic strategies against amyloid diseases. 相似文献
5.
Study of immobilized metal affinity chromatography sorbents for the analysis of peptides by on‐line solid‐phase extraction capillary electrophoresis‐mass spectrometry
下载免费PDF全文
![点击此处可从《Electrophoresis》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Lorena Ortiz‐Martin Fernando Benavente Silvia Medina‐Casanellas Estela Giménez Victoria Sanz‐Nebot 《Electrophoresis》2015,36(6):962-970
Several commercial immobilized metal affinity chromatography sorbents were evaluated in this study for the analysis of two small peptide fragments of the amyloid β‐protein (Aβ) (Aβ(1–15) and Aβ(10–20) peptides) by on‐line immobilized metal affinity SPE‐CE (IMA‐SPE‐CE). The performance of a nickel metal ion (Ni(II)) sorbent based on nitrilotriacetic acid as a chelating agent was significantly better than two copper metal ion (Cu(II)) sorbents based on iminodiacetic acid. A BGE of 25 mM phosphate (pH 7.4) and an eluent of 50 mM imidazole (in BGE) yielded a 25‐fold and 5‐fold decrease in the LODs by IMA‐SPE‐CE‐UV for Aβ(1–15) and Aβ(10–20) peptides (0.1 and 0.5 μg/mL, respectively) with regard to CE‐UV (2.5 μg/mL for both peptides). The phosphate BGE was also used in IMA‐SPE‐CE‐MS, but the eluent needed to be substituted by a 0.5% HAc v/v solution. Under optimum preconcentration and detection conditions, reproducibility of peak areas and migration times was acceptable (23.2 and 12.0%RSD, respectively). The method was more sensitive for Aβ(10–20) peptide, which could be detected until 0.25 μg/mL. Linearity for Aβ(10–20) peptide was good in a narrow concentration range (0.25–2.5 μg/mL, R2 = 0.93). Lastly, the potential of the optimized Ni(II)‐IMA‐SPE‐CE‐MS method for the analysis of amyloid peptides in biological fluids was evaluated by analyzing spiked plasma and serum samples. 相似文献
6.
Qiang Li Dr. Lei Liu Shuai Zhang Meng Xu Xueqin Wang Prof. Chen Wang Prof. Flemming Besenbacher Prof. Mingdong Dong 《Chemistry (Weinheim an der Bergstrasse, Germany)》2014,20(24):7236-7240
Graphene oxide (GO) is utilized as the modulator to tune the formation and development of amyloid fibrils (Aβ33–42). Atomic force microscopy temporal evolution measurements reveal that the initial binding between the peptide monomer and the large available surface of the GO sheets can redirect the assembly pathway of amyloid beta. The results support the possibility to develop graphene‐based materials to inhibit amyloidosis. 相似文献
7.
Capillary electrophoretic studies on quantum dots and histidine appended peptides self‐assembly
下载免费PDF全文
![点击此处可从《Electrophoresis》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Jianhao Wang Jingyan Li Yao Chen Yiwan Teng Cheli Wang Jinchen Li Li Liu Bingyu Dong Lin Qiu Pengju Jiang 《Electrophoresis》2015,36(19):2419-2424
Herein, we designed four peptides appended with different numbers of histidine (Hisn‐peptide). We launched a systematic investigation on quantum dots (QDs) and Hisn‐peptide self‐assembly in solution using fluorescence coupled CE (CE‐FL). The results indicated that CE‐FL was a powerful method to probe how ligands interaction on the surface of nanoparticles. The self‐assembly of QDs and peptide was determined by the numbers of histidine. We also observed that longer polyhistidine tags (n ≤ 6) could improve the self‐assembly efficiency. Furthermore, the formation and separation of QD‐peptide assembly were also studied by CE‐FL inside a capillary. The total time for the mixing, self‐assembly, separation, and detection was less than 10 min. Our method greatly expands the application of CE‐FL in QDs‐based biolabeling and bioanalysis. 相似文献
8.
Interaction of PiB‐Derivative Metal Complexes with Beta‐Amyloid Peptides: Selective Recognition of the Aggregated Forms
下载免费PDF全文
![点击此处可从《Chemistry (Weinheim an der Bergstrasse, Germany)》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Dr. André F. Martins David M. Dias Dr. Jean‐François Morfin Dr. Sara Lacerda Dr. Douglas V. Laurents Dr. Éva Tóth Prof. Carlos F. G. C. Geraldes 《Chemistry (Weinheim an der Bergstrasse, Germany)》2015,21(14):5413-5422
Metal complexes are increasingly explored as imaging probes in amyloid peptide related pathologies. We report the first detailed study on the mechanism of interaction between a metal complex and both the monomer and the aggregated form of Aβ1–40 peptide. We have studied lanthanide(III) chelates of two PiB‐derivative ligands (PiB=Pittsburgh compound B), L1 and L2, differing in the length of the spacer between the metal‐complexing DO3A macrocycle (DO3A= 1,4,7,10‐tetraazacyclododecane‐1,4,7‐triacetic acid) and the peptide‐recognition PiB moiety. Surface plasmon resonance (SPR) and saturation transfer difference (STD) NMR spectroscopy revealed that they both bind to aggregated Aβ1–40 (KD=67–160 μM ), primarily through the benzothiazole unit. HSQC NMR spectroscopy on the 15N‐labeled, monomer Aβ1–40 peptide indicates nonsignificant interaction with monomeric Aβ. Time‐dependent circular dichroism (CD), dynamic light scattering (DLS), and TEM investigations of the secondary structure and of the aggregation of Aβ1–40 in the presence of increasing amounts of the metal complexes provide coherent data showing that, despite their structural similarity, the two complexes affect Aβ fibril formation distinctly. Whereas GdL1, at higher concentrations, stabilizes β‐sheets, GdL2 prevents aggregation by promoting α‐helical structures. These results give insight into the behavior of amyloid‐targeted metal complexes in general and contribute to a more rational design of metal‐based diagnostic and therapeutic agents for amyloid‐ associated pathologies. 相似文献
9.
Isaak Beyer Dr. Nasrollah Rezaei‐Ghaleh Dr. Hans‐Wolfgang Klafki Dr. Olaf Jahn Dr. Ute Haußmann Prof. Dr. Jens Wiltfang Prof. Dr. Markus Zweckstetter Prof. Dr. Hans‐Joachim Knölker 《Chemistry (Weinheim an der Bergstrasse, Germany)》2016,22(25):8685-8693
In addition to the prototypic amyloid‐β (Aβ) peptides Aβ1–40 and Aβ1–42, several Aβ variants differing in their amino and carboxy termini have been described. Synthetic availability of an Aβ variant is often the key to study its role under physiological or pathological conditions. Herein, we report a protocol for the efficient solid‐phase peptide synthesis of the N‐terminally elongated Aβ‐peptides Aβ?3–38, Aβ?3–40, and Aβ?3–42. Biophysical characterization by NMR spectroscopy, CD spectroscopy, an aggregation assay, and electron microscopy revealed that all three peptides were prone to aggregation into amyloid fibrils. Immunoprecipitation, followed by mass spectrometry, indicated that Aβ?3–38 and Aβ?3–40 are generated by transfected cells even in the presence of a tripartite β‐site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor. The elongated Aβ peptides starting at Val(?3) can be separated from N‐terminally‐truncated Aβ forms by high‐resolution isoelectric‐focusing techniques, despite virtually identical isoelectric points. The synthetic Aβ variants and the methods presented here are providing tools to advance our understanding of the potential roles of N‐terminally elongated Aβ variants in Alzheimer's disease. 相似文献
10.
Microtubule‐Binding R3 Fragment from Tau Self‐Assembles into Giant Multistranded Amyloid Ribbons
下载免费PDF全文
![点击此处可从《Angewandte Chemie (International ed. in English)》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Dr. Jozef Adamcik Dr. Antoni Sánchez‐Ferrer Nadine Ait‐Bouziad Dr. Nicholas P. Reynolds Prof. Dr. Hilal A. Lashuel Prof. Dr. Raffaele Mezzenga 《Angewandte Chemie (International ed. in English)》2016,55(2):618-622
Tau protein and its fragments self‐assemble into amyloid fibrils in the presence of polyanions, such as heparin. By combining microscopy, scattering, and spectroscopy techniques, we studied the aggregation of the 26‐mer Tau‐derived peptide alone, Tau306–327, the third repeat fragment (R3) of the microtubule‐binding domain. We show that: i) the sole Tau306–327 can self‐assemble into amyloid fibrils without the need of aggregation‐promoting polyanions; ii) the resulting structures consist of surprisingly large, well‐ordered 2D laminated flat ribbons, with a log‐normal distribution of the lateral width, reaching the unprecedented lateral size of 350 nm and/or 45 individual protofilaments, that is, the largest amyloid laminated structures ever observed for Tau or any other amyloidogenic sequence. Our results provide insight into the molecular determinants of Tau aggregation and open new perspectives in the understanding of the assembly of amyloid fibrils and β‐sheet‐based biomaterials. 相似文献
11.
Hongyu Zhang Changlong Hao Aihua Qu Maozhong Sun Liguang Xu Chuanlai Xu Hua Kuang 《Angewandte Chemie (International ed. in English)》2020,59(18):7131-7138
The accumulation and deposition of β‐amyloid (Aβ) plaques in the brain is considered a potential pathogenic mechanism underlying Alzheimer's disease (AD). Chiral l/d ‐FexCuySe nanoparticles (NPs) were fabricated that interfer with the self‐assembly of Aβ42 monomers and trigger the Aβ42 fibrils in dense structures to become looser monomers under 808 nm near‐infrared (NIR) illumination. d ‐FexCuySe NPs have a much higher affinity for Aβ42 fibrils than l ‐FexCuySe NPs and chiral Cu2?xSe NPs. The chiral FexCuySe NPs also generate more reactive oxygen species (ROS) than chiral Cu2?xSe NPs under NIR‐light irradiation. In living MN9D cells, d ‐NPs attenuate the adhesion of Aβ42 to membranes and neuron loss after NIR treatment within 10 min without the photothermal effect. In‐vivo experiments showed that d ‐FexCuySe NPs provide an efficient protection against neuronal damage induced by the deposition of Aβ42 and alleviate symptoms in a mouse model of AD, leading to the recovery of cognitive competence. 相似文献
12.
Extracellular deposition of amyloid‐beta (Aβ) protein, a fragment of membrane glycoprotein called β‐amyloid precursor transmembrane protein (βAPP), is the major characteristic for the Alzheimer's disease (AD). However, the structural and mechanistic information of forming Aβ protein aggregates in a lag phase in cell exterior has been still limited. Here, we have performed multiple all‐atom molecular dynamics simulations for physiological 42‐residue amyloid‐beta protein (Aβ42) in explicit water to characterize most plausible aggregation‐prone structure (APS) for the monomer and the very early conformational transitions for Aβ42 protein misfolding process in a lag phase. Monitoring the early sequential conformational transitions of Aβ42 misfolding in water, the APS for Aβ42 monomer is characterized by the observed correlation between the nonlocal backbone H‐bond formation and the hydrophobic side‐chain exposure. Characteristics on the nature of the APS of Aβ42 allow us to provide new insight into the higher aggregation propensity of Aβ42 over Aβ40, which is in agreement with the experiments. On the basis of the structural features of APS, we propose a plausible aggregation mechanism from APS of Aβ42 to form fibril. The structural and mechanistic observations based on these simulations agree with the recent NMR experiments and provide the driving force and structural origin for the Aβ42 aggregation process to cause AD. © 2010 Wiley Periodicals, Inc. J Comput Chem, 2011 相似文献
13.
《Electroanalysis》2004,16(17):1407-1412
A three‐step sequential self‐assembly procedure was applied in preparing gold electrodes modified in a stable and controlled way by a monolayer of thiolated β‐cyclodextrin (β‐CD), with methylene blue (MB) included in its cavity as the active component of the monolayer, and octanethiol as the nonelectroactive spacer blocking the electrode surface not occupied by β‐CD. MB acted as a mediator of electrons with respect to a solution soluble analyte, H2O2, and provided electrical contact between the electrode and solution resident enzyme, laccase, catalyzing reduction of oxygen to water. 相似文献
14.
Hai‐tao Zhang Prof. Dr. Xiao‐dong Fan Prof. Dr. Wei Tian Rong‐tian Suo Zhen Yang Yang Bai Wan‐bin Zhang 《Chemistry (Weinheim an der Bergstrasse, Germany)》2015,21(13):5000-5008
The controlled secondary self‐assembly of amphiphilic molecules in solution is theoretically and practically significant in amphiphilic molecular applications. An amphiphilic β‐cyclodextrin (β‐CD) dimer, namely LA‐(CD)2, has been synthesized, wherein one lithocholic acid (LA) unit is hydrophobic and two β‐CD units are hydrophilic. In an aqueous solution at room temperature, LA‐(CD)2 self‐assembles into spherical micelles without ultrasonication. The primary micelles dissociates and then secondarily form self‐assemblies with branched structures under ultrasonication. The branched aggregates revert to primary micelles at high temperature. The ultrasound‐driven secondary self‐assembly is confirmed by transmission electron microscopy, dynamic light scattering, 1H NMR spectroscopy, and Cu2+‐responsive experiments. Furthermore, 2D NOESY NMR and UV/Vis spectroscopy results indicate that the formation of the primary micelles is driven by hydrophilic–hydrophobic interactions, whereas host–guest interactions promote the formation of the secondary assemblies. Additionally, ultrasonication is shown to be able to effectively destroy the primary hydrophilic–hydrophobic balances while enhancing the host–guest interaction between the LA and β‐CD moieties at room temperature. 相似文献
15.
Dr. Ling‐Yun Yang Dr. Xiao‐Bin Fu Dr. Tai‐Qiang Chen Prof. Li‐Kun Pan Dr. Peng Ji Prof. Ye‐Feng Yao Prof. Qun Chen 《Chemistry (Weinheim an der Bergstrasse, Germany)》2015,21(17):6346-6349
Highly conductive, crystalline, polymer electrolytes, β‐cyclodextrin (β‐CD)–polyethylene oxide (PEO)/LiAsF6 and β‐CD–PEO/NaAsF6, were prepared through supramolecular self‐assembly of PEO, β‐CD, and LiAsF6/NaAsF6. The assembled β‐CDs form nanochannels in which the PEO/X+ (X=Li, Na) complexes are confined. The nanochannels provide a pathway for directional motion of the alkali metal ions and, at the same time, separate the cations and the anions by size exclusion. 相似文献
16.
Co‐existence of Two Different α‐Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry
下载免费PDF全文
![点击此处可从《Angewandte Chemie (International ed. in English)》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Dr. Wojciech Paslawski Simon Mysling Karen Thomsen Dr. Thomas J. D. Jørgensen Prof. Dr. Daniel E. Otzen 《Angewandte Chemie (International ed. in English)》2014,53(29):7560-7563
Neurodegenerative disorders are characterized by the formation of protein oligomers and amyloid fibrils, which in the case of Parkinson’s disease involves the protein α‐synuclein (αSN). Cytotoxicity is mainly associated with the oligomeric species, but we still know little about their assembly and structure. Hydrogen/deuterium exchange (HDX) monitored by mass spectrometry is used to analyze oligomers formed by wild‐type (wt) αSN and also three familial αSN mutants (A30P, E46K, and A53T). All four variants show co‐existence of two different oligomers. The backbone amides of oligomer type I are protected from exchange with D2O until they dissociate into monomeric αSN by EX1 exchange kinetics. Fewer residues are protected against exchange in oligomer type II, but this type does not revert to αSN monomers. Both oligomers are protected in the core sequence Y39–A89. Based on incubation studies, oligomer type I appears to form straight fibrils, while oligomer type II forms amorphous clusters that do not directly contribute to the fibrillation process. 相似文献
17.
《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2017,129(33):9948-9951
Amyloid‐β peptide (Aβ) isoforms of different lengths and aggregation propensities coexist in vivo. These different isoforms are able to nucleate or frustrate the assembly of each other. N‐terminally truncated Aβ(11–40) and Aβ(11–42) make up one fifth of plaque load yet nothing is known about their interaction with full‐length Aβ(1–40/42). We show that in contrast to C‐terminally truncated isoforms, which do not co‐fibrillize, deletions of ten residues from the N terminus of Aβ have little impact on its ability to co‐fibrillize with the full‐length counterpart. As a consequence, N‐terminally truncated Aβ will accelerate fiber formation and co‐assemble into short rod‐shaped fibers with its full‐length Aβ counterpart. This has implications for the assembly kinetics, morphology, and toxicity of all Aβ isoforms. 相似文献
18.
Alexis Nazabal Simone Hornemann Adriano Aguzzi Renato Zenobi 《Journal of mass spectrometry : JMS》2009,44(6):965-977
Understanding the structural basis that distinguishes the amyloid form of the prion protein from its monomeric homologue is of crucial importance to elucidate the mechanism of the lethal diseases related to this protein. Recently, an in vitro conversion system was established which reproduces the transition of recombinant prion protein PrP(23–230) from its native α‐helical rich form into an aggregated amyloid β‐sheet rich form with physicochemical properties reminiscent to those of the disease‐related isoform of the prion protein, PrPSc. To study the tertiary and quaternary structural organization within recombinant amyloid fibrils from mouse, mPrP(23–231)βf; bovine, bPrP(23–230)βf; and elk, ePrP(23–230)βf; we utilized hydrogen/deuterium (H/D) exchange analyzed by matrix‐assisted laser desorption/ionization (MALDI) and nano‐electrospray (nano‐ESI) mass spectrometry. No significant differences were found by measuring the deuterium exchange kinetics of the aggregated fibrillar forms for mPrP(23–231)βf, bPrP(23–230)βf and ePrP(23–230)βf, indicating a similar overall structural organization of the fibrils from all three species. Next, we characterized the solvent accessibility for the soluble and fibrillar forms of the mouse prion protein by hydrogen exchange, pepsin proteolysis and nano‐ESI ion trap mass spectrometry analysis. In its amyloid form, two highly protected regions of mPrP(23–231) comprising residues [24–98] and [182–212] were identified. The residues between the two highly protected stretches were found to be more solvent exposed, but less than in the soluble protein, and might therefore rather form part of a fibrillar interface. Copyright © 2009 John Wiley & Sons, Ltd. 相似文献
19.
Yuko Murakoshi Dr. Tsuyoshi Takahashi Prof. Dr. Hisakazu Mihara 《Chemistry (Weinheim an der Bergstrasse, Germany)》2013,19(14):4525-4531
Aggregation of amyloid β‐peptide (Aβ) is closely related to the pathogenesis of Alzheimer’s disease (AD). Although much effort has been devoted to the construction of molecules that inhibit the aggregation of Aβ1‐42, high doses are needed for the inhibition of Aβ aggregation in many cases. Previously, we reported that designed green fluorescent protein (GFP) analogues that gives pseudo‐Aβ β‐sheet structures can work as an aggregation inhibitor against Aβ. To further test this design strategy, we constructed protein analogues that mimic Aβ β‐sheet structures of amyloids by using insulin‐like growth factor 2 receptor domain 11 (IGF2R‐d11) as a scaffold. A designed protein, named IG11KK, which has a parallel configuration of Aβ‐like β sheets, can bind more preferentially to oligomeric Aβ1‐42 than the monomer. Moreover, IG11KK suppressed the aggregation of Aβ1‐42 efficiently, even though lower concentrations of IG11KK than Aβ were used. The aggregation kinetics of Aβ in the presence of the designed proteins revealed that IG11KK can work as an inhibitor not only for the early to middle stages, but also in the latter stage of Aβ aggregation owing to its favorable binding to oligomeric structures of Aβ. The design strategy using β‐barrel proteins such as IGF2R‐d11 and GFP is useful in generating excellent inhibitors of protein misfolding and amyloid formation. 相似文献
20.
Yi‐Hong Chiu Jui‐Hsiang Liu 《Journal of polymer science. Part A, Polymer chemistry》2010,48(15):3368-3374
A novel achiral monomer end‐capped with a phenyl‐[1,3,4]oxadiazolyl group and threaded through β‐cyclodextrin was synthesized to investigate the host‐guest interactions in the inclusion complex. 1H NMR studies revealed that one or two cyclodextrin molecules were threaded onto the synthesized achiral monomer, leading to the formation of a fibrous construction of self‐assembled inclusion complexes. The formation of a self‐assembled inclusion complex was identified using SEM and TEM. The highly ordered alignment of self‐assembled supramolecules was confirmed using polarized optical microscopy. We demonstrate an easy process for the fabrication of nano‐structured self‐assembled inclusion complexes in pyridine/ethanol (1 mL/10 mL) as well as the enhancement of photo‐induced fluorescence via monomers end‐capped with a phenyl‐[1,3,4]oxadiazolyl moiety threaded with β‐cyclodextrins. © 2010 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 48: 3368–3374, 2010 相似文献