%0 Journal Article %1 LbL2009lyoph %A Qu, Xue %A Komatsu, Teruyuki %D 2010 %J ACS Nano %K LbL filtration japanese lyophilization %N 1 %P 563-573 %R 10.1021/nn901474y %T Molecular Capture in Protein Nanotubes %U http://pubs.acs.org/doi/abs/10.1021/nn901474y %V 4 %X We describe molecular capturing properties of protein nanotubes with a controllable ligand binding affinity and size selectivity. These practical biocylinders were prepared using an alternating layer-by-layer (LbL) assembly of protein and oppositely charged poly(amino acid) into the nanoporous polycarbonate (PC) membrane (pore diameter, 400 nm), with subsequent dissolution of the template. The tube wall typically comprises six layers of poly-l-arginine (PLA) and human serum albumin (HSA) (PLA/HSA)3. Use of high molecular weight PLA (Mw = ca. 70 000) yielded robust nanotubes, which are available as lyophilized powder. The (PLA/HSA)3 nanotubes swelled considerably in water, although the outer diameter was almost unaltered. Uranyl ion, 3,3′-diethylthiacarbocyanine iodide, and zinc(II) protoporphyrin IX (ZnPP) were bound to the HSA component in the cylinder wall. Similar nanotubes comprising recombinant HSA mutant rHSA(His), which has a strong binding affinity for ZnPP, captured this ligand more tightly. Furthermore, addition of excess myristic acid released ZnPP from the tubes through a ligand replacement reaction. The hybrid nanotubes bearing a single avidin layer as an internal surface captured FITC-biotin efficiently. Biotin-labeled nanoparticles are also incorporated into the tubes when their particle size is sufficiently small to enter the pores. Subsequent TEM observation revealed a line of loaded nanoparticles (100 nm) in the one-dimensional space interior.

@article{LbL2009lyoph, abstract = { We describe molecular capturing properties of protein nanotubes with a controllable ligand binding affinity and size selectivity. These practical biocylinders were prepared using an alternating layer-by-layer (LbL) assembly of protein and oppositely charged poly(amino acid) into the nanoporous polycarbonate (PC) membrane (pore diameter, 400 nm), with subsequent dissolution of the template. The tube wall typically comprises six layers of poly-l-arginine (PLA) and human serum albumin (HSA) [(PLA/HSA)3]. Use of high molecular weight PLA (Mw = ca. 70 000) yielded robust nanotubes, which are available as lyophilized powder. The (PLA/HSA)3 nanotubes swelled considerably in water, although the outer diameter was almost unaltered. Uranyl ion, 3,3′-diethylthiacarbocyanine iodide, and zinc(II) protoporphyrin IX (ZnPP) were bound to the HSA component in the cylinder wall. Similar nanotubes comprising recombinant HSA mutant [rHSA(His)], which has a strong binding affinity for ZnPP, captured this ligand more tightly. Furthermore, addition of excess myristic acid released ZnPP from the tubes through a ligand replacement reaction. The hybrid nanotubes bearing a single avidin layer as an internal surface captured FITC-biotin efficiently. Biotin-labeled nanoparticles are also incorporated into the tubes when their particle size is sufficiently small to enter the pores. Subsequent TEM observation revealed a line of loaded nanoparticles (100 nm) in the one-dimensional space interior. }, added-at = {2011-05-17T23:16:19.000+0200}, author = {Qu, Xue and Komatsu, Teruyuki}, biburl = {https://www.bibsonomy.org/bibtex/2d27e0cddafe9fb06d59d9f17fddc1800/saghi}, description = {Molecular Capture in Protein Nanotubes - ACS Nano (ACS Publications)}, doi = {10.1021/nn901474y}, eprint = {http://pubs.acs.org/doi/pdf/10.1021/nn901474y}, interhash = {eea51f1a90066bfe830831ff20bf78f1}, intrahash = {d27e0cddafe9fb06d59d9f17fddc1800}, journal = {ACS Nano}, keywords = {LbL filtration japanese lyophilization}, note = {PMID: 20020754}, number = 1, pages = {563-573}, timestamp = {2011-05-20T08:14:42.000+0200}, title = {Molecular Capture in Protein Nanotubes}, url = {http://pubs.acs.org/doi/abs/10.1021/nn901474y}, volume = 4, year = 2010 }