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

ACS Omega

School of Chemical and Biological Engineering, and Department of Materials Science and Engineering, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea.

Published: April 2018

AI Article Synopsis

  • Self-assembled nanostructures made from tyrosine-rich peptides have useful applications in biocatalysis, organic films, and membranes.
  • The study focuses on controlling the self-assembly of a specific peptide sequence (YYACAYY) to create large, thick nanofilms using Langmuir-Blodgett and Langmuir-Schaefer techniques.
  • The Tyr-C7mer peptide demonstrated surfactant-like behavior, enabling the successful creation and characterization of uniform nanofilms with redox properties, facilitated by silver nanoparticles assembly without additives.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6641360PMC
http://dx.doi.org/10.1021/acsomega.8b00395DOI Listing

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