Glycine Substitution Effects on the Supramolecular Morphology and Rigidity of Cell‐Adhesive Amphiphilic Peptides. Issue 59 (29th August 2019)
- Record Type:
- Journal Article
- Title:
- Glycine Substitution Effects on the Supramolecular Morphology and Rigidity of Cell‐Adhesive Amphiphilic Peptides. Issue 59 (29th August 2019)
- Main Title:
- Glycine Substitution Effects on the Supramolecular Morphology and Rigidity of Cell‐Adhesive Amphiphilic Peptides
- Authors:
- Ishida, Atsuya
Watanabe, Go
Oshikawa, Mio
Ajioka, Itsuki
Muraoka, Takahiro - Abstract:
- Abstract: Self‐assembling peptides that are capable of adopting β‐sheet structures can generate nanofibers that lead to hydrogel formation. Herein, to tune the supramolecular morphologies, mechanical properties, and stimuli responses of the hydrogels, we investigated glycine substitution in a β‐sheet‐forming amphiphilic peptide. Glycine substitution generally enhances conformational flexibility. Indeed, glycine substitution in an amphiphilic peptide weakened the hydrogels or even inhibited the gelation. However, unexpectedly, glycine substitution at the center of the peptide molecule significantly enhanced the hydrogel stiffness. The central glycine substitution affected the molecular packing and led to twisted β‐sheet structures and to nanofiber bundling, which likely led to the stiffened hydrogel. Importantly, the supramolecular structures were accurately predicted by molecular dynamics simulations, demonstrating the helpfulness of these techniques for the identification of self‐assembling peptides. The hydrogel formed by the amphiphilic peptide with the central glycine substitution had cell adhesive function, and showed a reversible thermal gel‐to‐sol transition. Thus, glycine substitution is effective in modulating self‐assembling structures, rheological properties, and dynamics of biofunctional self‐assembling peptides. Abstract : Bring on the substitute : Glycine substitution in a self‐assembling bioactive peptide affects the higher‐order structure and leads to theAbstract: Self‐assembling peptides that are capable of adopting β‐sheet structures can generate nanofibers that lead to hydrogel formation. Herein, to tune the supramolecular morphologies, mechanical properties, and stimuli responses of the hydrogels, we investigated glycine substitution in a β‐sheet‐forming amphiphilic peptide. Glycine substitution generally enhances conformational flexibility. Indeed, glycine substitution in an amphiphilic peptide weakened the hydrogels or even inhibited the gelation. However, unexpectedly, glycine substitution at the center of the peptide molecule significantly enhanced the hydrogel stiffness. The central glycine substitution affected the molecular packing and led to twisted β‐sheet structures and to nanofiber bundling, which likely led to the stiffened hydrogel. Importantly, the supramolecular structures were accurately predicted by molecular dynamics simulations, demonstrating the helpfulness of these techniques for the identification of self‐assembling peptides. The hydrogel formed by the amphiphilic peptide with the central glycine substitution had cell adhesive function, and showed a reversible thermal gel‐to‐sol transition. Thus, glycine substitution is effective in modulating self‐assembling structures, rheological properties, and dynamics of biofunctional self‐assembling peptides. Abstract : Bring on the substitute : Glycine substitution in a self‐assembling bioactive peptide affects the higher‐order structure and leads to the formation of bundled supramolecular nanofibers, enhances the stiffness of the hydrogel, and endows the system with a thermal response that shows a reversible gel‐to‐sol transition (see figure). … (more)
- Is Part Of:
- Chemistry. Volume 25:Issue 59(2019)
- Journal:
- Chemistry
- Issue:
- Volume 25:Issue 59(2019)
- Issue Display:
- Volume 25, Issue 59 (2019)
- Year:
- 2019
- Volume:
- 25
- Issue:
- 59
- Issue Sort Value:
- 2019-0025-0059-0000
- Page Start:
- 13523
- Page End:
- 13530
- Publication Date:
- 2019-08-29
- Subjects:
- amphiphiles -- gels -- molecular dynamics -- peptides -- self-assembly
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1521-3765 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/chem.201902083 ↗
- Languages:
- English
- ISSNs:
- 0947-6539
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3168.860500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 17492.xml