Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy
- Chinese Academy of Sciences, Shanghai (China)
- The Univ. of Texas at Austin, Austin, TX (United States)
- Stony Brook Univ., Stony Brook, NY (United States)
- Shanghai Jiao Tong Univ., Shanghai (China)
- Chinese Academy of Sciences, Shanghai (China); Shanghai Tech Univ., Shanghai (China)
- Huashan Hospital of Fudan Univ., Shanghai (China)
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
- Tufts Univ., Medford, MA (United States)
- Chinese Academy of Sciences, Shanghai (China); The Univ. of Texas at Austin, Austin, TX (United States); Shanghai Tech Univ., Shanghai (China)
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.
- Research Organization:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division
- Grant/Contract Number:
- AC02-05CH11231
- OSTI ID:
- 1526492
- Journal Information:
- Nature Communications, Vol. 7, Issue 1; ISSN 2041-1723
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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