Cited by 277Silk-based biomaterials and applicationsGraphite, nuclear technology, radiation studiesGraphene research and applications

Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein

Open access
Cho, Se Youn, Yun, Young Soo, Lee, Sungho, Jang, Dawon, Park, Kyu-Young, Kim, Jae Kyung, Kim, Byung Hoon, Kang, Kisuk +2 more·2015·Nature Communications

Abstract

Silk proteins are of great interest to the scientific community owing to their unique mechanical properties and interesting biological functionality. In addition, the silk proteins are not burned out following heating, rather they are transformed into a carbonaceous solid, pyroprotein; several studies have identified potential carbon precursors for state-of-the-art technologies. However, no mechanism for the carbonization of proteins has yet been reported. Here we examine the structural and chemical changes of silk proteins systematically at temperatures above the onset of thermal degradation. We find that the β-sheet structure is transformed into an sp2-hybridized carbon hexagonal structure by simple heating to 350 °C. The pseudographitic crystalline layers grew to form highly ordered graphitic structures following further heating to 2,800 °C. Our results provide a mechanism for the thermal transition of the protein and demonstrate a potential strategy for designing pyroproteins using a clean system with a catalyst-free aqueous wet process for in vivo applications.

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  • Silk fabrics can be transformed into highly conductive, intrinsically nitrogen-doped, flexible, and structure-maintained carbon textiles through thermal treatment.

    “Recently, it has been reported that silk fabrics can be transformed into highly conductive, intrinsically nitrogen-doped, flexible, and structure-maintained carbon textiles through thermal treatment (30–35).”

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Research works printed but not linked: 1

  1. Jenkins G. M. & Kawamura K. Polymeric carbons—carbon fibre, glass and char Cambridge Univ. Press (1976).

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Authors
Cho, S. Y., Yun, Y. S., Lee, S., Jang, D., Park, K.-Y., Kim, J. K., Kim, B. H., Kang, K., Kaplan, D. L., & Jin, H.-J.
Affiliations
  • Inha University (KR)
  • Korea Institute of Science and Technology (KR)
  • Seoul National University (KR)
  • Incheon National University (KR)
  • Tufts University (US)
Corresponding author
Jin, Hyoung-Joon
Venue
Nature Communications
Published
2015-05-20
Volume
6
Issue
1
Pages
7145-7145
ISSN
2041-1723 (ISSN-L)
OpenAlex
W2259787847
Cited by
277
References
30
Citations by year
2026: 21 · 2025: 25 · 2024: 38 · 2023: 21 · 2022: 28 · 2021: 29 · 2020: 29 · 2019: 28 · 2018: 24 · 2017: 17 · 2016: 15 · 2015: 2
FWCI
7.00
Type
journal article
Language
en
Open access
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • Seoul National University Open Repository (Seoul National University) (submittedVersion)
Funders
  • National Research Foundation
  • Korea Institute of Science and Technology
  • National Research Foundation of Korea (2010-C1AAA001-0029018, 2014R1A1A1002467, NRF-2013R1A1A2A10008534, NRF-2010-C1AAA001-0029018, NRF-2014R1A1A1002467)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
  • Physical Sciences › Materials Science › Materials Chemistry › Graphite, nuclear technology, radiation studies
  • Physical Sciences › Materials Science › Materials Chemistry › Graphene research and applications
Keywords
silk proteins, carbonization, beta-sheet, graphitic carbon, thermal degradation, carbon precursors, catalyst-free synthesis
MeSH terms
Animals, Calorimetry, Differential Scanning, Carbon, Catalysis, Crystallization, Fibroins, Hot Temperature, Microscopy, Electron, Scanning, Bombyx, X-Ray Diffraction, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Silk

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