Front Cover: Glycine Substitution Effects on the Supramolecular Morphology and Rigidity of Cell‐Adhesive Amphiphilic Peptides (Chem. Eur. J. 59/2019). Issue 59 (4th September 2019)

• Record Type: Journal Article
• Authors: Ishida, Atsuya; Watanabe, Go; Oshikawa, Mio; Ajioka, Itsuki; Muraoka, Takahiro
• Is Part Of: Chemistry. Volume 25:Issue 59(2019)
• Page Start: 13444
• Page End: 13444
• Publication Date: 2019-09-04
• Subjects: amphiphiles -- gels -- molecular dynamics -- peptides -- self-assembly; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201903870
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : Glycine substitution at the center of an amphiphilic peptide, which generally increases conformational flexibility and disturbs self‐assembly, allowed the formation of a hydrogel with enhanced stiffness. The central glycine substitution affected the packing to form a twisted β‐sheet and nanofiber bundling, which likely stiffened the hydrogel. The supramolecular structure was well predicted by molecular dynamics simulations. The hydrogel of the glycine‐substituted amphiphilic peptide had cell‐adhesive function, and showed a reversible thermal gel‐to‐sol transition. More information can be found in the Full Paper by T. Muraoka et al. on page 13523 .