Effect of Photoinduced Size Changes on Protein Refolding and Transport Abilities of Soft Nanotubes.
Self-assembly of azobenzene-modified amphiphiles (Glyn Azo, n=1-3) in water at room temperature in the presence of a protein produced nanotubes with the protein encapsulated in the channels. The Gly2 Azo nanotubes (7 nm internal diameter [i.d.]) promoted refolding of some encapsulated proteins, whereas the Gly3 Azo nanotubes (13 nm i.d.) promoted protein aggregation. Although the 20 nm i.d. channels of the Gly1 Azo 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 Gly1 Azo 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 Gly2 Azo 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.
Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan. n-kameta@aist.go.jp.
Naohiro
N
Kameta
Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan.
Haruhisa
H
Akiyama
Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan.
Mitsutoshi
M
Masuda
AIST Fellow, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan.
Toshimi
T
Shimizu
D000818:Animals; D001391:Azo Compounds / Q000737:chemistry*; D002256:Carbonic Anhydrases / Q000737:chemistry*; D002417:Cattle; D004800:Enzymes, Immobilized / Q000737:chemistry; D005998:Glycine / Q000031:analogs & derivatives*; D007536:Isomerism; D008027:Light; D008958:Models, Molecular; D043942:Nanotubes / Q000737:chemistry* / Q000648:ultrastructure; D055668:Photochemical Processes; D011489:Protein Denaturation; D058849:Protein Refolding; D013501:Surface-Active Agents / Q000737:chemistry*
D001391:Azo Compounds; D004800:Enzymes, Immobilized; D013501:Surface-Active Agents; D002256:Carbonic Anhydrases; C009850:azobenzene; D005998:Glycine
nanotubes; photochemistry; proteins; refolding; supramolecular chemistry