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• W3201323441 endingPage "10899" @default.
• W3201323441 startingPage "10893" @default.
• W3201323441 abstract "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." @default.
• W3201323441 created "2021-09-27" @default.
• W3201323441 creator A5030793270 @default.
• W3201323441 creator A5065667748 @default.
• W3201323441 creator A5089162978 @default.
• W3201323441 date "2021-09-24" @default.
• W3201323441 modified "2023-10-02" @default.
• W3201323441 title "Cosolvents Restrain Self-Assembly of a Fibroin-Like Peptide on Graphite" @default.
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• W3201323441 doi "https://doi.org/10.1021/acs.jpcb.1c02594" @default.
• W3201323441 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34559528" @default.
• W3201323441 hasPublicationYear "2021" @default.
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