Development of an artificial chaperone system based on cyclodextrin.
Molecular chaperones in living systems inspired us to explore new concepts for assisting protein refolding. The chaperone selectively interacts with a non-native protein by hydrophobic interaction to prevent irreversible aggregation and releases the protein in its refolded form with the aid of ATP and another co-chaperone. Cyclodextrins have been used to simulate the function of the chaperones by controlling the hydrophobic interaction with proteins. In this chapter, we review the cyclodextrin (CD)-related protein refolding systems.
Sasaki
Yoshihiro
Y
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
Akiyoshi
Kazunari
K
D040761:Biomimetic Materials / Q000737:chemistry*; D003505:Cyclodextrins / Q000737:chemistry*; D002479:Inclusion Bodies / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry* / Q000302:isolation & purification*
D003505:Cyclodextrins; D018832:Molecular Chaperones; D011994:Recombinant Proteins