Enzyme-responsive artificial chaperone system with amphiphilic amylose primer.
An enzyme-responsive artificial chaperone system which employs an amphiphilic amylose primer (dodecyl maltopentaose, C12-MP) as a surfactant and phosphorylase b was designed to enable protein refolding. Effective refolding of carbonic anhydrase B after both heat denaturation (70 degrees C for 10min) and guanidine hydrochloride (6M) denaturation was observed by controlled association between the protein molecules and the C12-MP primer micelle through an enzymatic reaction.
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
Nobuyuki
N
Morimoto
Naruhito
N
Ogino
Tadashi
T
Narita
Kazunari
K
Akiyoshi
D000688:Amylose / Q000737:chemistry*; D024401:Carbonic Anhydrase I / Q000737:chemistry; D019791:Guanidine / Q000494:pharmacology; D006358:Hot Temperature; D018832:Molecular Chaperones / Q000737:chemistry*; D015394:Molecular Structure; D010763:Phosphorylase b / Q000737:chemistry; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D013501:Surface-Active Agents / Q000737:chemistry
D018832:Molecular Chaperones; D013501:Surface-Active Agents; D000688:Amylose; D010763:Phosphorylase b; D024401:Carbonic Anhydrase I; D019791:Guanidine