Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy.
Nan QinShaoqing ZhangJianjuan JiangStephanie N Gilbert CorderZhigang QianZhitao ZhouWoonsoo LeeKeyin LiuXiaohan WangXinxin LiZhifeng ShiYing MaoHans A BechtelMichael C MartinXiaoxia XiaBenedetto MarelliDavid L KaplanFiorenzo G OmenettoMengkun LiuTiger H TaoPublished in: Nature communications (2016)
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.
Keyphrases
- high resolution
- single molecule
- atomic force microscopy
- tissue engineering
- wound healing
- molecular dynamics simulations
- amino acid
- binding protein
- molecular dynamics
- electron microscopy
- solar cells
- endothelial cells
- mass spectrometry
- high speed
- oxidative stress
- diabetic rats
- quantum dots
- photodynamic therapy
- drug induced