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Corrigendum to “Peptide backbone-copper ring structure: A molecular insight into copper-induced amyloid toxicity”
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作者 王静 姜先凯 +9 位作者 苏秀榕 周星飞 王宇 王耿 耿和平 姜政 黄方 陈刚 王春雷 方海平 《Chinese Physics B》 SCIE EI CAS CSCD 2023年第6期716-716,共1页
The author list originally given in Wang et al. Chin. Phys. B 31 108702 (2022) has been amended to remove four authors, Hua Li, Bin Wu, Jun Guo and Chenqi Xu, who believe their contributions are more suitable to be cr... The author list originally given in Wang et al. Chin. Phys. B 31 108702 (2022) has been amended to remove four authors, Hua Li, Bin Wu, Jun Guo and Chenqi Xu, who believe their contributions are more suitable to be credited in the acknowledgments. 展开更多
关键词 interactions between metal ion and protein quantum chemistry calculation protein aggregation amyloid diseases
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Peptide backbone-copper ring structure:A molecular insight into copper-induced amyloid toxicity
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作者 Jing Wang Hua Li +13 位作者 Xiankai Jiang Bin Wu Jun Guo Xiurong Su Xingfei Zhou Yu Wang Geng Wang Heping Geng Zheng Jiang Fang Huang Gang Chen Chunlei Wang Haiping Fang Chenqi Xu 《Chinese Physics B》 SCIE EI CAS CSCD 2022年第10期288-296,共9页
Copper ions can promote amyloid diseases that are associated with amyloid peptides, such as type 2 diabetes(T2D),Alzheimer's disease(AD), Parkinson's disease(PD), and amyotrophic lateral sclerosis(ALS). Howeve... Copper ions can promote amyloid diseases that are associated with amyloid peptides, such as type 2 diabetes(T2D),Alzheimer's disease(AD), Parkinson's disease(PD), and amyotrophic lateral sclerosis(ALS). However, the underlying molecular mechanism remains obscure. Here we present that Cu^(2+)is able to specifically bind to the backbone of T2D related human islet amyloid polypeptide(hIAPP) by forming a ring structure, which causes the reduction of Cu^(2+)to Cu^(+) to produce reactive oxygen species(ROS) and the modulation of hIAPP aggregation. Nuclear magnetic resonance spectroscopy showed that Cu^(2+)bound to the backbone of a turn region, His18-Ser21, which is critical for hIAPP aggregation.Ab initio calculations and x-ray absorption fine structure analyses revealed that Cu^(2+)simultaneously bound with both the amide nitrogen and carbonyl oxygen on the peptide backbone, resulting in a ring structure, and causing the reduction of Cu^(2+)to Cu^(+) to form a hIAPP-Cu^(+) complex. 2′,7′-dichlorodihydrofluorescin diacetate fluorescence measurements further indicated that this complex led to enhanced ROS levels in rat insulinoma cells. Additionally, thioflavin T fluorescence and atomic force microscopy measurements denoted that the backbone-Cu ring structure largely modulated hIAPP aggregation,including the inhibition of hIAPP fibrillation and the promotion of peptide oligomerization. These findings shed new light on the molecular mechanism of Cu^(2+)-induced amyloid toxicity involving both the enhancement of ROS and the modulation of hIAPP aggregation. 展开更多
关键词 interactions between metal ion and protein quantum chemistry calculation protein aggregation amyloid diseases
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Methodology and Foreground of Metallomics
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作者 He Bin Jiang Guibin 《Science Foundation in China》 CAS 2005年第2期36-41,共6页
Metallomics is proposed as a new omics to fol- low genomics, proteomics and metabolomics. This paper gives an overview of the development of met- allomics based on the introduction of the concept of metallomics and it... Metallomics is proposed as a new omics to fol- low genomics, proteomics and metabolomics. This paper gives an overview of the development of met- allomics based on the introduction of the concept of metallomics and its methodology. 展开更多
关键词 metalLOMICS combination of metal and protein chemical composition metallomes SPECIATION
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