Acyl cystamine: Small-molecular foldase mimics accelerating oxidative refolding of disulfide-containing proteins

摘要: Based on the structural characteristic of Protein disulfide isomerases and DsbA that have hydrophobic regions around active sites, alkyl tails are linked to cystamine create new small molecular foldase mimics, acyl cystamine. Both oxidizing power oxidation specificity enhanced by n-octanoyl or n-hexanoyl tail. N-octanoyl very effective facilitate oxidative protein refolding at strong reducing environments. In presence 0.42 mM DTT, activity recovery lysozyme is over 90% 90-min with 0.1 as oxidant, while almost no recovered 0.2 GSSG 160-min refolding. For mg/mL lysozyme, 0.6 1.12 residual DTT redox agents, reaches high 93% after for only 20 min. ribonuclease A (RNase A) refolding, 0.4 1.30 within 3 h. Thus, oxidants, necessity remove excess in reduced denatured solutions can be greatly alleviated. With a moderate hydrophobicity, promising application an extensive concentration range. It observed RNase A, about half needed when compared achieve same kinetic effect. © 2011 American Institute Chemical Engineers Biotechnol. Prog.,