Fmoc-diphenylalanine self assembles to a hydrogel via a novel architecture based on π-π interlocked β-sheets


Autoria(s): Smith, Andrew M.; Williams, Richard J.; Tang, Claire; Coppo, Paolo; Collins, Richard F.; Turner, Michael L.; Saiani, Alberto; Ulijn, Rein V.
Data(s)

01/01/2008

Resumo

The self assembly of peptide hydrogelators that carry aromatic substituents can be modeled by a novel nanocylindrical architecture. The proposed model suggests that the nanocylinders are formed by anti-parallel β-sheets interlocked by the π-stacking interactions of fluorenyl groups and phenyl rings. This explanation is consistent with the structures observed in TEM and the data obtained by a variety of spectroscopic techniques. <br />

Identificador

http://hdl.handle.net/10536/DRO/DU:30047748

Idioma(s)

eng

Publicador

Wiley - VCH Verlag GmbH & Co. KGaA

Relação

http://dro.deakin.edu.au/eserv/DU:30047748/williams-fmocdiphenylalanine-2008.pdf

http://dx.doi.org/10.1002/adma.200701221

Direitos

2008, WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim

Palavras-Chave #biomaterials #hydrogels #peptides #self-assembly
Tipo

Journal Article