Self-assembled arginine-capped peptide bolaamphiphile nanosheets for cell culture and controlled wettability surfaces


Autoria(s): da Silva, Emerson Rodrigo; Walter, Merlin Nathaniel Mark; Reza, Mehedi; Castelletto, Valeria; Ruokolainen, Janne; Connon, Che John; Alves, Wendel Andrade; Hamley, Ian William
Data(s)

08/09/2015

Resumo

The spontaneous assembly of a peptide bolaamphiphile in water, namely, RFL4FR (R, arginine; F, phenylalanine; L, leucine) is investigated, along with its novel properties in surface modification and usage as substrates for cell culture. RFL4FR self-assembles into nanosheets through lateral association of the peptide backbone. The L4 sequence is located within the core of the nanosheets, whereas the R moieties are exposed to the water at the surface of the nanosheets. Kinetic assays indicate that the self-assembly is driven by a remarkable two-step process, where a nucleation phase is followed by fast growth of nanosheets with an autocatalysis process. The internal structure of the nanosheets is formed from ultrathin bolaamphiphile monolayers with a crystalline orthorhombic symmetry with cross-β organization. We show that human corneal stromal fibroblast (hCSF) cells can grow on polystyrene films coated with films dried from RFL4FR solutions. For the first time, this type of amphiphilic peptide is used as a substrate to modulate the wettability of solid surfaces for cell culture applications.

Formato

text

Identificador

http://centaur.reading.ac.uk/51161/1/acs%252Ebiomac%252E5b00820.pdf

da Silva, E. R., Walter, M. N. M., Reza, M., Castelletto, V., Ruokolainen, J., Connon, C. J., Alves, W. A. and Hamley, I. W. (2015) Self-assembled arginine-capped peptide bolaamphiphile nanosheets for cell culture and controlled wettability surfaces. Biomacromolecules, 16 (10). pp. 3180-3190. ISSN 1525-7797 doi: 10.1021/acs.biomac.5b00820 <http://dx.doi.org/10.1021/acs.biomac.5b00820>

Idioma(s)

en

Publicador

American Chemical Society

Relação

http://centaur.reading.ac.uk/51161/

http://dx.doi.org/10.1021/acs.biomac.5b00820

10.1021/acs.biomac.5b00820

Direitos

cc_by_nc_nd

Tipo

Article

PeerReviewed