Effect of Photoinduced Size Changes on Protein Refolding and Transport Abilities of Soft Nanotubes |
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Authors: | Dr. Naohiro Kameta Dr. Haruhisa Akiyama Dr. Mitsutoshi Masuda Dr. Toshimi Shimizu |
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Affiliation: | 1. Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki, Japan;2. AIST Fellow, National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki, Japan |
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Abstract: | Self‐assembly of azobenzene‐modified amphiphiles (GlynAzo, n=1–3) in water at room temperature in the presence of a protein produced nanotubes with the protein encapsulated in the channels. The Gly2Azo nanotubes (7 nm internal diameter [i.d.]) promoted refolding of some encapsulated proteins, whereas the Gly3Azo nanotubes (13 nm i.d.) promoted protein aggregation. Although the 20 nm i.d. channels of the Gly1Azo nanotubes were too large to influence the encapsulated proteins, narrowing of the i.d. to 1 nm by trans‐to‐cis photoisomerization of the azobenzene units of the Gly1Azo monomers packed in the solid bilayer membranes led to a squeezing out of the proteins into the bulk solution and simultaneously enhanced their refolding ratios. In contrast, photoinduced transformation of the Gly2Azo nanotubes to short nanorings (<40 nm) with a large i.d. (28 nm) provided no further refolding assistance. We thus demonstrate that pertubation by the solid bilayer membrane wall of the nanotubes is important to accelerate refolding of the denatured proteins during their transport in the narrow nanotube channels. |
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Keywords: | nanotubes photochemistry proteins refolding supramolecular chemistry |
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