Introduction of D-Glutamate at a Critical Residue of A beta 42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity

Warner Christopher J. A.; Dutta Subrata; Foley Alejandro R.; Raskatov Jevgenij A.

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Introduction of D-Glutamate at a Critical Residue of A beta 42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity

机译：在β42的关键残基处引入D-谷氨酸可稳定原纤维聚集体，并增强毒性

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The amyloid beta peptide 42 (A beta 42) is an aggregation-prone peptide that plays a pivotal role in Alzheimer's disease. We report that a subtle perturbation to the peptide through a single chirality change at glutamate 22 leads to a pronounced delay in the beta-sheet adoption of the peptide. This was accompanied by an attenuated propensity of the peptide to form fibrils, which was correlated with changes at the level of the fibrillary architecture. Strikingly, the incorporation of D-glutamate was found to stabilize a soluble, ordered macromolecular assembly with enhanced cytotoxicity to PC12 cells, highlighting the importance of advanced prefibrillary A beta aggregates in neurotoxicity.

机译：淀粉样蛋白β肽42（A beta 42）是一种易于聚集的肽，在阿尔茨海默氏病中起关键作用。我们报告说，通过在谷氨酸22处的单个手性变化，对肽的微妙扰动导致肽的β-折叠采用明显延迟。这伴随着肽形成原纤维的倾向减弱，这与原纤维结构水平的变化相关。令人惊讶地，发现D-谷氨酸的掺入稳定了可溶的，有序的大分子组装体，对PC12细胞具有增强的细胞毒性，突显了先进的原纤维前Aβ聚集体在神经毒性中的重要性。

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《Chemistry: A European journal》 |2016年第34期|共4页
作者
Warner Christopher J. A.; Dutta Subrata; Foley Alejandro R.; Raskatov Jevgenij A.;
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正文语种 eng
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关键词
aggregation; Alzheimer's disease; amyloid beta peptide; chirality; neurotoxicity;

机译：聚集;阿尔茨海默氏病;淀粉样β肽;手性;神经毒性;

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1. Introduction of D-Glutamate at a Critical Residue of A beta 42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity [J] . Warner Christopher J. A., Dutta Subrata, Foley Alejandro R., Chemistry: A European journal . 2016,第34期

机译：在β42的关键残基处引入D-谷氨酸可稳定原纤维聚集体，并增强毒性
2. A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates [J] . Galante Denise, Ruggeri Francesco Simone, Dietler Giovanni, The international journal of biochemistry and cell biology . 2016,第Null期

机译：临界浓度的N端焦谷氨酰淀粉样β驱动Ab1-42错折叠成毒性更大的聚集体
3. Amyloid-peptide beta 42 Enhances the Oligomerization and Neurotoxicity of apoE4: The C-terminal Residues Leu279, Lys282 and Gln284 Modulate the Structural and Functional Properties of apoE4 [J] . Dafnis Ioannis, Argyri Letta, Chroni Angeliki Neuroscience: An International Journal under the Editorial Direction of IBRO . 2018,第期

机译：淀粉样蛋白肽β22增强了ApoE4的低聚和神经毒性：C-末端残基Leu279，Lys282和GLN284调节apoE4的结构和功能性质
4. Deletion of the gene encoding for the enzyme Methionine sulphoxide reductase A increases the toxicity of Abeta (1-42) in an in vivo model. [C] . Minniti A., Inestrosa N. and Aldunate R. International Conference on Alzheimer's and Parkinson's Diseases . 2009

机译：缺失对酶甲硫氨酸硫氧化物还原酶A的基因增加了体内模型中ABETA（1-42）的毒性。
5. Amyloid beta-peptide (1-42)-mediated oxidative stress and neurotoxicity: I. The role of methionine 35. II. Proteomic identification of specifically oxidized proteins in models of Alzheimer's disease. [D] . Boyd-Kimball, Debra Lynn. 2004

机译：淀粉样β-肽（1-42）介导的氧化应激和神经毒性：I.蛋氨酸的作用35. II。蛋白质组学鉴定阿尔茨海默病模型中特定氧化的蛋白质。
6. Introduction of d‐Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity [O] . Dr. Christopher J. A. Warner, Dr. Subrata Dutta, Alejandro R. Foley, -1

机译：在Aβ42的关键残基处引入d-谷氨酸盐可稳定原纤维聚集体并增强毒性
7. Systematic A beta Analysis in Drosophila Reveals High Toxicity for the 1-42, 3-42 and 11-42 Peptides, and Emphasizes N- and C-Terminal Residues [O] . Jonsson, Maria, Pokrzywa, Malgorzata, Starkenberg, Annika, 2015

机译：果蝇中的系统性A beta分析揭示了1-42、3-42和11-42肽的高毒性，并强调了N和C末端残基

Introduction of D-Glutamate at a Critical Residue of A beta 42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity

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