Mechanism of Nucleated Conformational Conversion of A beta 42

Fu Ziao; Aucoin Darryl; Davis Judianne; Van Nostrand William E.; Smith Steven

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Mechanism of Nucleated Conformational Conversion of A beta 42

机译：A beta 42的有核构象转换的机制

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Soluble oligorners and protofibrils of the A beta 42 peptide are neurotoxic intermediates in the conversion of monomeric A beta 42 into the amyloid fibrils associated with Alzheimer's disease. Nuclear magnetic resonance and Fourier transform infrared spectroscopy, along with single-touch atomic force microscopy, are used to establish the structural transitions involved in fibril formation. We show that under conditions favorable for the nucleated conformation conversion, the A beta 42 peptide aggregates into largely unstructured low-molecular weight (MW) oligomers that are able to stack to form high-MW oligomers and to laterally associate to form protofibrils. beta-Sheet secondary structure develops during the irreversible lateral association of the oligomers. The first step in this conversion is the formation of an antiparallel beta-hairpin stabilized by intramonomer hydrogen bonding. The antiparallel beta-hairpins then associate into a cross beta-sheet structure with parallel and in-register beta-strands having intermonomer hydrogen bonding.

机译：Aβ42肽的可溶性寡聚体和原纤维是将Aβ42单体转化为与阿尔茨海默氏病相关的淀粉样蛋白原纤维的神经毒性中间体。核磁共振和傅里叶变换红外光谱，以及单触原子力显微镜，可用于建立涉及原纤维形成的结构转变。我们表明，在有利于核构象转化的条件下，Aβ42肽聚集成很大程度上无结构的低分子量（MW）低聚物，能够堆叠形成高MW低聚物并横向缔合以形成原纤维。 β-Sheet二级结构在寡聚物不可逆的横向缔合过程中形成。该转化的第一步是通过单体内氢键稳定的反平行β-发夹的形成。然后，反平行的β-发夹结合成具有平行的和在寄存器内的具有单体间氢键的β-链的交叉β-折叠结构。

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《Biochemistry》 |2015年第27期|共11页
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Fu Ziao; Aucoin Darryl; Davis Judianne; Van Nostrand William E.; Smith Steven;
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2. High-frequency (50 Hz) electroacupuncture ameliorates cognitive impairment in rats with amyloid beta 1-42-induced Alzheimer's disease [J] . Chao-Chao Yu, Ying Wang, Feng Shen, 中国神经再生研究（英文版） . 2018,第010期
3. Hyperoside protects the blood-brain barrier from neurotoxicity of amyloid beta 1–42 [J] . Chen-Yang Liu, Kuan Bai, Xiao-Hui Liu, 中国神经再生研究（英文版） . 2018,第011期
4. Protective effects of components of the Chinese herb grassleaf sweetlfag rhizome on PC12 cells incubated with amyloid-beta42 [J] . Zi-hao Liang, Xiao-hui Cheng, Zhi-gang Ruan, 中国神经再生研究（英文版） . 2015,第008期
5. Mechanism of Nucleated Conformational Conversion of A beta 42 [J] . Fu Ziao, Aucoin Darryl, Davis Judianne, Biochemistry . 2015,第27期

机译：A beta 42的有核构象转换的机制
6. Exploration of the mechanism for LPFFD inhibiting the formation of beta-sheet conformation of A beta(1-42) in water [J] . Yang C, Zhu XL, Li JY, Journal of molecular modeling . 2010,第4期

机译：LPFFD抑制水中A beta（1-42）β-折叠构象形成机理的探索
7. The mechanisms of flavonoids inhibiting conformational transition of amyloid-beta(42) monomer: a comparative molecular dynamics simulation study [J] . Wang Ling, Zeng Ranran, Pang Xiaoqian, RSC Advances . 2015,第81期

机译：抑制淀粉样蛋白β（42）单体抑制构象过渡的黄酮类化合物：比较分子动力学模拟研究
8. FT-IR studies on the effect of beta-sheet breaker peptides on the conformation and aggregational properties of beta-amyloid1-42 and Prp106-126 [C] . Eva Lement, Marta Zarandi, Katalin Soos, European Peptide Symposium . 2002

机译：FT-IR研究β-薄片破碎肽对β-淀粉样蛋白1-42和PRP的构象和聚集性能的影响106-126
9. I. Selection, synthesis, and mechanisms studies of cell-penetrating peptides: New drug delivery systems. II. Biological lessons for the preparation of Abeta(1-42) and cyclic peptide probe for the detection of botulinum neurotoxin A. [D] . Kim, YoungSoo. 2006

机译：I.细胞穿透肽的选择，合成和机理研究：新药物递送系统。二。制备Abeta（1-42）和用于检测肉毒杆菌神经毒素A的环肽探针的生物学课程。
10. Amyloid-β Forms Fibrils by Nucleated Conformational Conversion of Oligomers [O] . Jiyong Lee, Elizabeth K. Culyba, Evan T. Powers, -1

机译：β淀粉样原纤维形式由低聚物的有核象转换
11. The alfa to beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of the beta conformation seeding. [O] . S. TOMASELLI, V. ESPOSITO, P. VANGONE, 2006

机译：阿尔茨海默氏症abeta-（1-42）肽在水性介质中的α到β构象转变是可逆的：逐步构象分析表明β构象接种的位置。
12. Mechanism of Conversion of Light into Chemical Energy in Bacteriorhodopsin: Identification of Charge Movements and Coupling to Active Site Conformational Changes [R] . Dratz, E. A. 1988

机译：细菌视紫红质中光转化为化学能的机制：电荷运动的识别和活性位点构象变化的耦合

Mechanism of Nucleated Conformational Conversion of A beta 42

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