共查询到20条相似文献,搜索用时 66 毫秒
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Yunxiang Sun Aleksandr Kakinen Yanting Xing Pouya Faridi Aparna Nandakumar Anthony W. Purcell Thomas P. Davis Pu Chun Ke Feng Ding 《Small (Weinheim an der Bergstrasse, Germany)》2019,15(18)
The self‐assembly of human islet amyloid polypeptide (hIAPP) into β‐sheet‐rich nanofibrils is associated with the pathogeny of type 2 diabetes. Soluble hIAPP is intrinsically disordered with N‐terminal residues 8–17 as α‐helices. To understand the contribution of the N‐terminal helix to the aggregation of full‐length hIAPP, here the oligomerization dynamics of the hIAPP fragment 8–20 (hIAPP8‐20) are investigated with combined computational and experimental approaches. hIAPP8‐20 forms cross‐β nanofibrils in silico from isolated helical monomers via the helical oligomers and α‐helices to β‐sheets transition, as confirmed by transmission electron microscopy, atomic force microscopy, circular dichroism spectroscopy, Fourier transform infrared spectroscopy, and reversed‐phase high performance liquid chromatography. The computational results also suggest that the critical nucleus of aggregation corresponds to hexamers, consistent with a recent mass‐spectroscopy study of hIAPP8‐20 aggregation. hIAPP8‐20 oligomers smaller than hexamers are helical and unstable, while the α‐to‐β transition starts from the hexamers. Converted β‐sheet‐rich oligomers first form β‐barrel structures as intermediates before aggregating into cross‐β nanofibrils. This study uncovers a complete picture of hIAPP8‐20 peptide oligomerization, aggregation nucleation via conformational conversion, formation of β‐barrel intermediates, and assembly of cross‐β protofibrils, thereby shedding light on the aggregation of full‐length hIAPP, a hallmark of pancreatic beta‐cell degeneration. 相似文献
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Carbon Nanodot‐Sensitized Modulation of Alzheimer's β‐Amyloid Self‐Assembly,Disassembly, and Toxicity
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You Jung Chung Kayoung Kim Byung Il Lee Chan Beum Park 《Small (Weinheim an der Bergstrasse, Germany)》2017,13(34)
The self‐assembly of amyloidogenic peptides into β‐sheet‐rich aggregates is a general feature of many neurodegenerative diseases, including Alzheimer's disease, which signifies the need for the effective attenuation of amyloid aggregation toward alleviating amyloid‐associated neurotoxicity. This study reports that photoluminescent carbon nanodots (CDs) can effectively suppress Alzheimer's β‐amyloid (Aβ) self‐assembly and function as a β‐sheet breaker disintegrating preformed Aβ aggregates. This study synthesizes CDs using ammonium citrate through one‐pot hydrothermal treatment and passivates their surface with branched polyethylenimine (bPEI). The bPEI‐coated CDs (bPEI@CDs) exhibit hydrophilic and cationic surface characteristics, which interact with the negatively charged residues of Aβ peptides, suppressing the aggregation of Aβ peptides. Under light illumination, bPEI@CDs display a more pronounced effect on Aβ aggregation and on the dissociation of β‐sheet‐rich assemblies through the generation of reactive oxygen species from photoactivated bPEI@CDs. The light‐triggered attenuation effect of Aβ aggregation using a series of experiments, including photochemical and microscopic analysis, is verified. Furthermore, the cell viability test confirms the ability of photoactivated bPEI@CDs for the suppression of Aβ‐mediated cytotoxicity, indicating bPEI@CDs' potency as an effective anti‐Aβ neurotoxin agent. 相似文献
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H. Fujiwara H.‐J. Lee H.‐B. Cui H. Kobayashi E. Fujiwara A. Kobayashi 《Advanced materials (Deerfield Beach, Fla.)》2004,16(19):1765-1769
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Andreas Kobus 《真空研究与实践》2000,12(2):99-102
The accurate design of condensers in the vacuum technology with the help of 'real' flash calculation is possible due to the easy access to calculation programs and databases. The article shows with a simple example, how important the knowledge of the real condensation‐behaviour can be, when designing a modern, effluent reduced vacuum system. In addition, design failures on vacuum condensers can cause trouble in the performance of vacuum pumps. 相似文献