Glycolipid-based nanostructures with thermal-phase transition behavior functioning as solubilizers and refolding accelerators for protein aggregates.

作者: N. Kameta , T. Matsuzawa , K. Yaoi , J. Fukuda , M. Masuda

DOI: 10.1039/C7SM00310B

关键词:

摘要: The self-assembly of synthetic glycolipids produced nanostructures such as vesicles and nanotubes consisting bilayer membranes, which underwent a gel-to-liquid crystalline thermal phase transition. Vesicles formed at temperatures above the transition (Tg-l) could solubilize aggregates denatured proteins by trapping them in fluid membranes. Cooling to below Tg-l caused morphological transformation into that accompanied from solid state. This phenomenon allowed trapped be quickly released bulk solution simultaneously facilitated refolding proteins. efficiency strongly depended on electrostatic attraction between membranes Because long shape (>400 nm) nanotubes, simple membrane filtration through pore size 200 nm led complete separation recovery refolded (3-9 sizes).

参考文章(72)
P.A. Srere, [1] Citrate synthase Citric Acid Cycle. ,vol. 13, pp. 3- 11 ,(1969) , 10.1016/0076-6879(69)13005-0
Kentaro Shiraki, Motonori Kudou, Shingo Nishikori, Harue Kitagawa, Tadayuki Imanaka, Masahiro Takagi, Arginine ethylester prevents thermal inactivation and aggregation of lysozyme FEBS Journal. ,vol. 271, pp. 3242- 3247 ,(2004) , 10.1111/J.1432-1033.2004.04257.X
Tai Hirakura, Yuta Nomura, Yasuhiro Aoyama, Kazunari Akiyoshi, Photoresponsive nanogels formed by the self-assembly of spiropyrane-bearing pullulan that act as artificial molecular chaperones. Biomacromolecules. ,vol. 5, pp. 1804- 1809 ,(2004) , 10.1021/BM049860O
Nuzhat Gull, Priyankar Sen, Rizwan Hasan Khan, Kabir-ud-Din, Interaction of bovine (BSA), rabbit (RSA), and porcine (PSA) serum albumins with cationic single-chain/gemini surfactants: a comparative study. Langmuir. ,vol. 25, pp. 11686- 11691 ,(2009) , 10.1021/LA901639H
Patrizia Polverino de Laureto, Erica Frare, Rossella Gottardo, Herman van Dael, Angelo Fontana, Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis Protein Science. ,vol. 11, pp. 2932- 2946 ,(2009) , 10.1110/PS.0205802
David L. Daugherty, David Rozema, Peter E. Hanson, Samuel H. Gellman, Artificial Chaperone-assisted Refolding of Citrate Synthase Journal of Biological Chemistry. ,vol. 273, pp. 33961- 33971 ,(1998) , 10.1074/JBC.273.51.33961
Ryoichi Kuboi, Seiichi Morita, Hideyuki Ota, Hiroshi Umakoshi, None, Protein refolding using stimuli-responsive polymer-modified aqueous two-phase systems Journal of Chromatography B: Biomedical Sciences and Applications. ,vol. 743, pp. 215- 223 ,(2000) , 10.1016/S0378-4347(00)00062-1
Fu-Gen Wu, Jun-Jie Luo, Zhi-Wu Yu, Unfolding and refolding details of lysozyme in the presence of β-casein micelles Physical Chemistry Chemical Physics. ,vol. 13, pp. 3429- 3436 ,(2011) , 10.1039/C0CP01184C