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Cosolvents Restrain Self-Assembly of a Fibroin-Like Peptide on Graphite

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journal contribution
posted on 24.09.2021, 18:41 by Robert Ccorahua, Hironaga Noguchi, Yuhei Hayamizu
Controllable self-assembly of peptides on solid surfaces has been investigated for establishing functional bio/solid interfaces. In this work, we study the influence of organic solvents on the self-assembly of a fibroin-like peptide on a graphite surface. The peptide has been designed by mimicking fibroin proteins to have strong hydrogen bonds among peptides enabling their self-assembly. We have employed cosolvents of water and organic solvents with a wide range of dielectric constants to control peptide self-assembly on the surface. Atomic force microscopy has revealed that the peptides self-assemble into highly ordered monolayer-thick linear structures on graphite after incubation in pure water, where the coverage of peptides on the surface is more than 85%. When methanol is mixed, the peptide coverage becomes zero at a threshold concentration of 30% methanol on graphite and 25% methanol on MoS2. The threshold concentration in ethanol, isopropanol, dimethyl sulfoxide, and acetone varies depending on the dielectric constant with restraining self-assembly of the peptides, and particularly low dielectric-constant protic solvents prevent the peptide self-assembly significantly. The observed phenomena are explained by competitive surface adsorption of the organic solvents and peptides and the solvation effect of the peptide assembly.

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