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Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold

Author

Listed:
  • Hyung-Seok Jang

    (School of Chemical and Biological Engineering, Seoul National University)

  • Jung-Ho Lee

    (School of Chemical and Biological Engineering, Seoul National University
    Seoul National University)

  • Yong-Sun Park

    (Seoul National University)

  • Young-O Kim

    (School of Chemical and Biological Engineering, Seoul National University)

  • Jimin Park

    (Seoul National University)

  • Tae-Youl Yang

    (Seoul National University)

  • Kyoungsuk Jin

    (Seoul National University)

  • Jaehun Lee

    (Seoul National University)

  • Sunghak Park

    (Seoul National University)

  • Jae Myoung You

    (School of Chemical and Biological Engineering, Seoul National University)

  • Ki-Woong Jeong

    (Konkuk University)

  • Areum Shin

    (Konkuk University)

  • In-Seon Oh

    (Inha University)

  • Min-Kyung Kwon

    (Inha University)

  • Yong-Il Kim

    (Korea Research Institute of Standards and Science)

  • Hoon-Hwe Cho

    (Seoul National University)

  • Heung Nam Han

    (Seoul National University)

  • Yangmee Kim

    (Konkuk University)

  • Yoon Ho Chang

    (Inha University)

  • Seung R. Paik

    (School of Chemical and Biological Engineering, Seoul National University)

  • Ki Tae Nam

    (Seoul National University)

  • Yoon-Sik Lee

    (School of Chemical and Biological Engineering, Seoul National University)

Abstract

In two-dimensional interfacial assemblies, there is an interplay between molecular ordering and interface geometry, which determines the final morphology and order of entire systems. Here we present the interfacial phenomenon of spontaneous facet formation in a water droplet driven by designed peptide assembly. The identified peptides can flatten the rounded top of a hemispherical droplet into a plane by forming a macroscopic two-dimensional crystal structure. Such ordering is driven by the folding geometry of the peptide, interactions of tyrosine and crosslinked stabilization by cysteine. We discover the key sequence motifs and folding structures and study their sequence-specific assembly. The well-ordered, densely packed, redox-active tyrosine units in the YYACAYY (H-Tyr-Tyr-Ala-Cys-Ala-Tyr-Tyr-OH) film can trigger or enhance chemical/electrochemical reactions, and can potentially serve as a platform to fabricate a molecularly tunable, self-repairable, flat peptide or hybrid film.

Suggested Citation

  • Hyung-Seok Jang & Jung-Ho Lee & Yong-Sun Park & Young-O Kim & Jimin Park & Tae-Youl Yang & Kyoungsuk Jin & Jaehun Lee & Sunghak Park & Jae Myoung You & Ki-Woong Jeong & Areum Shin & In-Seon Oh & Min-K, 2014. "Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4665
    DOI: 10.1038/ncomms4665
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    Cited by:

    1. Mengmeng Xia & Qiyue Wang & Yamin Liu & Chunyan Fang & Bo Zhang & Shengfei Yang & Fu Zhou & Peihua Lin & Mingzheng Gu & Canyu Huang & Xiaojun Zhang & Fangyuan Li & Hongying Liu & Guangfeng Wang & Dais, 2024. "Self-propelled assembly of nanoparticles with self-catalytic regulation for tumour-specific imaging and therapy," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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