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 (+10 others)
2014 Nature Communications  
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
more » ... ing 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.
doi:10.1038/ncomms4665 pmid:24722220 fatcat:mmss6ngpejevdaxkpkoz5kqjx4