DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
Rechercher
(titres de publication, de périodique et noms de colloque inclus)
2008-11-05 - Article/Dans un journal avec peer-review - Anglais - 8 page(s)

Matmour R., De Cat I., George S.J., Adriaens W., Leclère Philippe , Bomans P.H.H., Sommerdijk N.A.J.M., Gielen J.C., Christianen P.C.M., Heldens J.T., van Hest J.C.M., Lowik D.W.P.M., De Feyter S., Meijer E.W., Schenning A.P.H.J., "Oligo(p-phenylenevinylene)-Peptide Conjugates: Synthesis and Self-Assembly in Solution and at the Solid-Liquid Interface" in Journal of the American Chemical Society, 130, 44, 14576-14583

  • Edition : American Chemical Society, Washington (DC)
  • Codes CREF : Chimie des surfaces et des interfaces (DI1327), Physique de l'état condense [struct., électronique, etc.] (DI1266), Instrumentation et méthodes en physique (DI1270)
  • Unités de recherche UMONS : Chimie des matériaux nouveaux (S817)
  • Instituts UMONS : Institut de Recherche en Science et Ingénierie des Matériaux (Matériaux)
Texte intégral :

Abstract(s) :

(Anglais) Two oligo(p-phenylenevinylene)-peptide hybrid amphiphiles have been synthesized using solid- and liquid-phase strategies. The amphiliphiles are composed of a p-conjugated oligo(p-phenylenevinylene) trimer (OPV) which is coupled at either a glycinyl-alanyl-glycinyl-alanyl-glycine (GAGAG) silk-inspired ß-sheet or a glycinyl-alanyl-asparagyl-prolyl-asparagy-alanyl-alanyl-glycine (GANPNAAG) ß-turn forming oligopeptide sequence. The solid-phase strategy enables one to use longer peptides if strong acidic conditions are avoided, whereas the solution-phase coupling gives better yields. The study of the two-dimensional (2D) self-assembly of OPV-GAGAG by scanning tunneling microscopy (STM) at the submolecular level demonstrated the formation of bilayers in which the molecules are lying antiparallel in a ß-sheet conformation. In the case of OPV-GANPNAAG self-assembled monolayers could not be observed. Absorption, fluorescence, and circular dichroism studies showed that OPV-GAGAG and OPV-GANPNAAG are aggregated in a vaiety of organic solvents. In water cryogenic temperature transmission electron microscopy (cryo-TEM), atomic force microscopy (AFM), light scattering, and optical studies reveal that self-assembled nanofibers are formed in which the helical organization of the OPV segments is dictated by the peptide sequence.

Notes :
  • (Anglais) Publié en ligne le 11 octobre 2008
Identifiants :
  • DOI : 10.1021/ja803026j