원문정보
초록
영어
Poly-γ-glutamic acid-cholesterol conjugates that consists of poly-γ-glutamic acid (γ-PGA) as a hydrophilic backbone and cholesterol amine as a hydrophobic segment were synthesizedusing 1,1-carbonylbis-1H-imidazole (CDI). The synthesized γ-PGA-cholesterol conjugate formed the nanoparticle by the self-association in water. The size of the γ-PGA-cholesterol conjugate nanoparticle was a mean diameter ranging from 340 to 400 nm. The γ-PGA-cholesterol conjugate nanoparticle have the ability to trap and release protein by the host-guest interaction of the cholesteryl group and β-cyclodextrin, suggested the molecular chaperone activity for refolding of denatured protein. We studied the chaperone-like activity of γ-PGA-cholesterol conjugate nanoparticle by refolding of HA-M2 fusion protein. HA-M2 fusion protein was over-expressed as an insoluble form in E. coli. This insoluble protein was trapped in γ-PGA-cholesterol conjugate nanoparticle, and then, released by the host-guest interaction of the cholesteryl group and β-cyclodextrin. This released HA-M2 insoluble protein renatured at outside of γ-PGA-cholesterol conjugate nanoparticle by extended-release effect. [This work was supported by the 'Seoul R&BD Program(10580)’]