Tailoring a Tyrosine-Rich Peptide into Size- and Thickness-Controllable Nanofilms.

ABSTRACT: Self-assembled nanostructures of tyrosine-rich peptides have a number of potential applications such as biocatalysts, organic conducting films, and ion-selective membranes. In modulating a self-assembly process of peptides, the interfacial force is an important factor for kinetic control. Here, we present the formation of large-sized and thickness-controllable nanofilms from the YYACAYY peptide sequence (Tyr-C7mer peptide) using Langmuir-Blodgett and Langmuir-Schaefer deposition methods. The Tyr-C7mer peptide showed typical surfactant-like properties, which were demonstrated via the isotherm test (surface pressure-area) by spreading the Tyr-C7mer peptide solution onto an air/water interface. Uniform and flat peptide nanofilms were successfully fabricated and characterized. The redox activity of densely packed tyrosine moieties on the peptide nanofilm was also evaluated by assembling silver nanoparticles on the nanofilm without requiring any additives.

SUBMITTER: Paribok IV 

PROVIDER: S-EPMC6641360 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature