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Title: Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy

Abstract

Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures.

Authors:
 [1];  [2];  [1]; ORCiD logo [3];  [4];  [1];  [2];  [1];  [2];  [5];  [6];  [6];  [7]; ORCiD logo [7];  [4];  [8];  [9];  [9];  [3];  [10]
  1. Chinese Academy of Sciences, Shanghai (China)
  2. The Univ. of Texas at Austin, Austin, TX (United States)
  3. Stony Brook Univ., Stony Brook, NY (United States)
  4. Shanghai Jiao Tong Univ., Shanghai (China)
  5. Chinese Academy of Sciences, Shanghai (China); Shanghai Tech Univ., Shanghai (China)
  6. Huashan Hospital of Fudan Univ., Shanghai (China)
  7. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  8. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
  9. Tufts Univ., Medford, MA (United States)
  10. Chinese Academy of Sciences, Shanghai (China); The Univ. of Texas at Austin, Austin, TX (United States); Shanghai Tech Univ., Shanghai (China)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Scientific User Facilities Division
OSTI Identifier:
1526492
Grant/Contract Number:  
AC02-05CH11231
Resource Type:
Accepted Manuscript
Journal Name:
Nature Communications
Additional Journal Information:
Journal Volume: 7; Journal Issue: 1; Journal ID: ISSN 2041-1723
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY

Citation Formats

Qin, Nan, Zhang, Shaoqing, Jiang, Jianjuan, Corder, Stephanie Gilbert, Qian, Zhigang, Zhou, Zhitao, Lee, Woonsoo, Liu, Keyin, Wang, Xiaohan, Li, Xinxin, Shi, Zhifeng, Mao, Ying, Bechtel, Hans A., Martin, Michael C., Xia, Xiaoxia, Marelli, Benedetto, Kaplan, David L., Omenetto, Fiorenzo G., Liu, Mengkun, and Tao, Tiger H. Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy. United States: N. p., 2016. Web. doi:10.1038/ncomms13079.
Qin, Nan, Zhang, Shaoqing, Jiang, Jianjuan, Corder, Stephanie Gilbert, Qian, Zhigang, Zhou, Zhitao, Lee, Woonsoo, Liu, Keyin, Wang, Xiaohan, Li, Xinxin, Shi, Zhifeng, Mao, Ying, Bechtel, Hans A., Martin, Michael C., Xia, Xiaoxia, Marelli, Benedetto, Kaplan, David L., Omenetto, Fiorenzo G., Liu, Mengkun, & Tao, Tiger H. Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy. United States. doi:10.1038/ncomms13079.
Qin, Nan, Zhang, Shaoqing, Jiang, Jianjuan, Corder, Stephanie Gilbert, Qian, Zhigang, Zhou, Zhitao, Lee, Woonsoo, Liu, Keyin, Wang, Xiaohan, Li, Xinxin, Shi, Zhifeng, Mao, Ying, Bechtel, Hans A., Martin, Michael C., Xia, Xiaoxia, Marelli, Benedetto, Kaplan, David L., Omenetto, Fiorenzo G., Liu, Mengkun, and Tao, Tiger H. Fri . "Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy". United States. doi:10.1038/ncomms13079. https://www.osti.gov/servlets/purl/1526492.
@article{osti_1526492,
title = {Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy},
author = {Qin, Nan and Zhang, Shaoqing and Jiang, Jianjuan and Corder, Stephanie Gilbert and Qian, Zhigang and Zhou, Zhitao and Lee, Woonsoo and Liu, Keyin and Wang, Xiaohan and Li, Xinxin and Shi, Zhifeng and Mao, Ying and Bechtel, Hans A. and Martin, Michael C. and Xia, Xiaoxia and Marelli, Benedetto and Kaplan, David L. and Omenetto, Fiorenzo G. and Liu, Mengkun and Tao, Tiger H.},
abstractNote = {Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures.},
doi = {10.1038/ncomms13079},
journal = {Nature Communications},
number = 1,
volume = 7,
place = {United States},
year = {2016},
month = {10}
}

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Works referenced in this record:

Water-insoluble silk films with silk I structure
journal, April 2010


A Physically Transient Form of Silicon Electronics
journal, September 2012


Silk as a biomaterial
journal, August 2007