Self-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif
Visualitza/Obre
Self-assembly.pdf (604,2Kb) (Accés restringit)
Sol·licita una còpia a l'autor
Què és aquest botó?
Aquest botó permet demanar una còpia d'un document restringit a l'autor. Es mostra quan:
- Disposem del correu electrònic de l'autor
- El document té una mida inferior a 20 Mb
- Es tracta d'un document d'accés restringit per decisió de l'autor o d'un document d'accés restringit per política de l'editorial
Cita com:
hdl:2117/14443
Tipus de documentArticle
Data publicació2011-10-20
Condicions d'accésAccés restringit per política de l'editorial
Llevat que s'hi indiqui el contrari, els
continguts d'aquesta obra estan subjectes a la llicència de Creative Commons
:
Reconeixement-NoComercial-SenseObraDerivada 3.0 Espanya
Abstract
Self-assembly in aqueous solution has been investigated for two Fmoc [Fmoc = N-(fluorenyl)-9-methoxycarbonyl] tetrapeptides comprising the RGDS cell adhesion motif from fibronectin or the scrambled sequence GRDS. The hydrophobic Fmoc unit confers amphiphilicity on the molecules, and introduces aromatic stacking interactions. Circular dichroism and FTIR spectroscopy show that the self-assembly of both peptides at low concentration is dominated by interactions among Fmoc units, although Fmoc-GRDS shows β-sheet features, at lower concentration than Fmoc-RGDS. Fibre X-ray diffraction indicates β-sheet formation by both peptides at sufficiently high concentration. Strong alignment effects are revealed by linear dichroism experiments for Fmoc-GRDS. Cryo-TEM and small-angle X-ray scattering (SAXS) reveal that both samples form fibrils with a diameter of approximately 10 nm. Both Fmoc-tetrapeptides form self-supporting hydrogels at sufficiently high concentration. Dynamic shear rheometry enabled measurements of the moduli for the Fmoc-GRDS hydrogel, however syneresis was observed for the Fmoc-RGDS hydrogel which was significantly less stable to shear. Molecular dynamics computer simulations were carried out considering parallel and antiparallel β-sheet configurations of systems containing 7 and 21 molecules of Fmoc-RGDS or Fmoc-GRDS, the results being analyzed in terms of both intermolecular structural parameters and energy contributions.
CitacióCastelletto, V. [et al.]. Self-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif. "Soft matter", 20 Octubre 2011, vol. 7, núm. 2011, p. 11405-11415.
ISSN1744-683X
Versió de l'editorhttp://pubs.rsc.org/en/Content/ArticleLanding/2011/SM/c1sm06550e
Col·leccions
- GRPFM - Grup de Recerca en Propietats Físiques dels Materials - Articles de revista [20]
- IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies - Articles de revista [398]
- Departament de Física i Enginyeria Nuclear (fins octubre 2015) - Articles de revista [603]
- Departament d'Enginyeria Química - Articles de revista [2.212]
Fitxers | Descripció | Mida | Format | Visualitza |
---|---|---|---|---|
Self-assembly.pdf | 604,2Kb | Accés restringit |