Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix,Angewandte Chemie International Edition

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Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2018-01-11 , DOI: 10.1002/anie.201710642
Ruirui Xing ₁ , Chengqian Yuan _{1,

2} , Shukun Li _{1,

3} , Jingwen Song ₁ , Junbai Li ₄ , Xuehai Yan _{1,

2,

3}

Affiliation

Secondary structures such as α‐helix and β‐sheet are the major structural motifs within the three‐dimensional geometry of proteins. Therefore, structure transitions from β‐sheet to α‐helix not only can serve as an effective strategy for the therapy of neurological diseases through the inhibition of β‐sheet aggregation but also extend the application of α‐helix fibrils in biomedicine. Herein, we present a charge‐induced secondary structure transition of amyloid‐derived dipeptide assemblies from β‐sheet to α‐helix. We unravel that the electrostatic (charge) repulsion between the C‐terminal charges of the dipeptide molecules are responsible for the conversion of the secondary structure. This finding provides a new perspective to understanding the secondary structure formation and transformation in the supramolecular organization and life activity.

中文翻译：

淀粉样二肽组装体的电荷诱导二级结构从β-Sheet转变为α-Helix

二级结构（例如α螺旋和β折叠）是蛋白质三维几何结构中的主要结构基序。因此，从β-折叠结构转变为α-螺旋结构不仅可以通过抑制β-折叠结构聚集而成为治疗神经系统疾病的有效策略，而且可以扩展α-螺旋结构在生物医学中的应用。本文中，我们介绍了由淀粉样蛋白衍生的二肽组装体从β-折叠到α-螺旋的电荷诱导的二级结构转变。我们发现，二肽分子C端电荷之间的静电（电荷）排斥作用是二级结构的转化。这一发现为理解超分子组织和生活活动中二级结构的形成和转变提供了新的视角。

更新日期：2018-01-11

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