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; Yoon Sik Lee

doi:10.1038/ncomms4665

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 journal › Article › peer-review

88 Citations (Scopus)

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.

Original language	English
Article number	3665
Journal	Nature communications
Volume	5
DOIs	https://doi.org/10.1038/ncomms4665
Publication status	Published - 2014 Apr 11
Externally published	Yes

ASJC Scopus subject areas

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

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10.1038/ncomms4665

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Jang, H. S., Lee, J. H., Park, Y. S., Kim, Y. O., Park, J., Yang, T. Y., Jin, K., Lee, J., Park, S., You, J. M., Jeong, K. W., Shin, A., Oh, I. S., Kwon, M. K., Kim, Y. I., Cho, H. H., Han, H. N., Kim, Y., Chang, Y. H., ... Lee, Y. S. (2014). Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold. Nature communications, 5, Article 3665. https://doi.org/10.1038/ncomms4665

Jang, HS, Lee, JH, Park, YS, Kim, YO, Park, J, Yang, TY, Jin, K, Lee, J, Park, S, You, JM, Jeong, KW, Shin, A, Oh, IS, Kwon, MK, Kim, YI, Cho, HH, Han, HN, Kim, Y, Chang, YH, Paik, SR, Nam, KT & Lee, YS 2014, 'Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold', Nature communications, vol. 5, 3665. https://doi.org/10.1038/ncomms4665

@article{4db41a3047c144ea9e7bd6c783140443,

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

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.",

author = "Jang, {Hyung Seok} and Lee, {Jung Ho} and Park, {Yong Sun} and Kim, {Young O.} and Jimin Park and Yang, {Tae Youl} and Kyoungsuk Jin and Jaehun Lee and Sunghak Park and You, {Jae Myoung} and Jeong, {Ki Woong} and Areum Shin and Oh, {In Seon} and Kwon, {Min Kyung} and Kim, {Yong Il} and Cho, {Hoon Hwe} and Han, {Heung Nam} and Yangmee Kim and Chang, {Yoon Ho} and Paik, {Seung R.} and Nam, {Ki Tae} and Lee, {Yoon Sik}",

note = "Funding Information: We thank Hye-Rim So and Professor Han-Bin Oh in Sogang University for MALDI analysis. We also appreciate the comments from Professor Romas Kazlauskas in the University of Minnesota. This work is supported by the National Research Foundation of Korea (NRF) under the Ministry of Science, ICT and Future. We gratefully acknowledge the support of the Pioneer Research Center Program (2011-0027888) of NRF. K.T.N. thanks the support of the Basic Science Research (2011-0011225) and Global Frontier R&D program on Center for Multiscale Energy System (0420-20130104) and the Fusion Research Program for Green Technologies through NRF the National Research Foundation of Korea(NRF) funded by the Ministry of Science, ICT & Future (2012M3C1A1048863). H.N.H. was supported by Basic Science Research Programme through the National Research Foundation in Korea funded by the Ministry of Science, ICT and Future Planning (2013008806).",

year = "2014",

month = apr,

day = "11",

doi = "10.1038/ncomms4665",

language = "English",

volume = "5",

journal = "Nature communications",

issn = "2041-1723",

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TY - JOUR

T1 - Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold

AU - Jang, Hyung Seok

AU - Lee, Jung Ho

AU - Park, Yong Sun

AU - Kim, Young O.

AU - Park, Jimin

AU - Yang, Tae Youl

AU - Jin, Kyoungsuk

AU - Lee, Jaehun

AU - Park, Sunghak

AU - You, Jae Myoung

AU - Jeong, Ki Woong

AU - Shin, Areum

AU - Oh, In Seon

AU - Kwon, Min Kyung

AU - Kim, Yong Il

AU - Cho, Hoon Hwe

AU - Han, Heung Nam

AU - Kim, Yangmee

AU - Chang, Yoon Ho

AU - Paik, Seung R.

AU - Nam, Ki Tae

AU - Lee, Yoon Sik

N1 - Funding Information: We thank Hye-Rim So and Professor Han-Bin Oh in Sogang University for MALDI analysis. We also appreciate the comments from Professor Romas Kazlauskas in the University of Minnesota. This work is supported by the National Research Foundation of Korea (NRF) under the Ministry of Science, ICT and Future. We gratefully acknowledge the support of the Pioneer Research Center Program (2011-0027888) of NRF. K.T.N. thanks the support of the Basic Science Research (2011-0011225) and Global Frontier R&D program on Center for Multiscale Energy System (0420-20130104) and the Fusion Research Program for Green Technologies through NRF the National Research Foundation of Korea(NRF) funded by the Ministry of Science, ICT & Future (2012M3C1A1048863). H.N.H. was supported by Basic Science Research Programme through the National Research Foundation in Korea funded by the Ministry of Science, ICT and Future Planning (2013008806).

PY - 2014/4/11

Y1 - 2014/4/11

N2 - 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.

AB - 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.

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U2 - 10.1038/ncomms4665

DO - 10.1038/ncomms4665

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AN - SCOPUS:84898618725

SN - 2041-1723

VL - 5

JO - Nature communications

JF - Nature communications

M1 - 3665

ER -

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

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