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Self-Assembled Arginine-Capped Peptide Bolaamphiphile Nanosheets for Cell Culture and Controlled Wettability Surfaces
Author(s) -
Emerson Rodrigo da Silva,
Merlin Nathaniel Mark Walter,
Mehedi Reza,
Valeria Castelletto,
Janne Ruokolainen,
Che J. Con,
Wendel A. Alves,
Ian W. Hamley
Publication year - 2015
Publication title -
biomacromolecules
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.689
H-Index - 220
eISSN - 1526-4602
pISSN - 1525-7797
DOI - 10.1021/acs.biomac.5b00820
Subject(s) - chemistry , amphiphile , peptide , self assembly , monolayer , biophysics , polymer chemistry , chemical engineering , stereochemistry , materials science , biochemistry , copolymer , organic chemistry , engineering , biology , polymer
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.

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