Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding

Jadhav S, Amabili P, Stammler H-G, Sewald N (2017)
CHEMISTRY 23(43): 10352-10357.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Abstract / Bemerkung
Gabapentin, an antiepileptic drug, is known to form stable helical structures in short peptides. Distinctly, we report on the newly synthesized g-analogue of gabapentin, that is, gamma-gabapentin (gamma-Gpn), which manifests beta-sheet character at molecular and nanofibrous hydrogels at the supramolecular level. We investigated the influence of proximally immobilized cationic amino acids (lysine and arginine) on the self-assembly of backbone-expanded tripeptide motif. Interestingly, arginine was found to be superior, both physically and mechanically, over lysine in driving hydrogelation. We have concluded that intrinsic and biochemically distinct properties of the guanidinium ion of arginine (compared to ammonium ion of lysine) have contributed towards this effect. Furthermore, similar to pyroglutamyl (pGlu) modified amyloid beta peptides, N-pGlu modification of our self-assembling tripeptide motif exerts a dramatic influence on aggregation and exhibits enhanced beta-sheet character, accelerated self-assembly kinetics, improved optical transparency and provides higher mechanical stiffness to the peptide hydrogel.
Stichworte
biomaterial; foldamer; hydrogel; peptides; supramolecular chemistry
Erscheinungsjahr
2017
Zeitschriftentitel
CHEMISTRY
Band
23
Ausgabe
43
Seite(n)
10352-10357
ISSN
0947-6539
eISSN
1521-3765
Page URI
https://pub.uni-bielefeld.de/record/2916505

Zitieren

Jadhav S, Amabili P, Stammler H-G, Sewald N. Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding. CHEMISTRY. 2017;23(43):10352-10357.
Jadhav, S., Amabili, P., Stammler, H. - G., & Sewald, N. (2017). Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding. CHEMISTRY, 23(43), 10352-10357. doi:10.1002/chem.201701450
Jadhav, S., Amabili, P., Stammler, H. - G., and Sewald, N. (2017). Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding. CHEMISTRY 23, 10352-10357.
Jadhav, S., et al., 2017. Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding. CHEMISTRY, 23(43), p 10352-10357.
S. Jadhav, et al., “Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding”, CHEMISTRY, vol. 23, 2017, pp. 10352-10357.
Jadhav, S., Amabili, P., Stammler, H.-G., Sewald, N.: Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding. CHEMISTRY. 23, 10352-10357 (2017).
Jadhav, Sandip, Amabili, Paolo, Stammler, Hans-Georg, and Sewald, Norbert. “Remarkable Modulation of Self-Assembly in Short gamma-Peptides by Neighboring Ions and Orthogonal H-Bonding”. CHEMISTRY 23.43 (2017): 10352-10357.

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 28590582
PubMed | Europe PMC

Suchen in

Google Scholar