Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix. Issue 6 (11th January 2018)

• Record Type: Journal Article
• Authors: Xing, Ruirui; Yuan, Chengqian; Li, Shukun; Song, Jingwen; Li, Junbai; Yan, Xuehai
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 6(2018)
• Page Start: 1537
• Page End: 1542
• Publication Date: 2018-01-11
• Subjects: gels -- nanofibers -- peptides -- phase transitions -- self-assembly; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201710642
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : The supramolecular conformation of a peptide can be changed by charging a peptide building block. The self‐assembling short peptide Fmoc‐FF undergoes a conformation transformation from β‐sheet to α‐helix by tuning the charges of its C‐terminal domain, associated with cooperation of electrostatic repulsion and hydrogen‐bonding attraction.