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Lookup NU author(s): Merlin Walter, Professor Che ConnonORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
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.
Author(s): da Silva ER, Walter MNM, Reza M, Castelletto V, Ruokolainen J, Connon CJ, Alves WA, Hamley IW
Publication type: Article
Publication status: Published
Journal: Biomacromolecules
Year: 2015
Volume: 16
Issue: 10
Pages: 3180-3190
Print publication date: 12/10/2015
Online publication date: 08/09/2015
Acceptance date: 03/09/2015
Date deposited: 22/09/2015
ISSN (print): 1525-7797
ISSN (electronic): 1526-4602
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/acs.biomac.5b00820
DOI: 10.1021/acs.biomac.5b00820
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