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. PaikKi Tae Nam, Yoon Sik Lee

Research output: Contribution to journalArticlepeer-review

88 Citations (Scopus)


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.

Original languageEnglish
Article number3665
JournalNature communications
Publication statusPublished - 2014 Apr 11
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)


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