Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix |
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| Authors: | Dr Ruirui Xing Dr Chengqian Yuan Dr Shukun Li Dr Jingwen Song Prof Dr Junbai Li Prof Xuehai Yan |
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| Affiliation: | 1. http://www.yan‐assembly.org/;2. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China;3. Center for Mesoscience, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China;4. University of Chinese Academy of Sciences, Beijing, China;5. Key Laboratory of Colloid and Interface Science, Center for Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing, China |
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| Abstract: | 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. |
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| Keywords: | gels nanofibers peptides phase transitions self-assembly |
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