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

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-Kyung Kwon, Yong-Il Kim, Hoon-Hwe Cho, Heung Nam Han, Yangmee Kim, Yoon Ho Chang, Seung R. Paik, Ki Tae Nam () and Yoon-Sik Lee ()
Additional contact information
Hyung-Seok Jang: School of Chemical and Biological Engineering, Seoul National University
Jung-Ho Lee: School of Chemical and Biological Engineering, 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

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms4665

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