A newly proposed mechanism for arginine-assisted protein refolding--not inhibiting soluble oligomers although promoting a correct structure
| Autor: | Yongdong Liu, Zhiguo Su, Jingjing Li, Jing Chen, Peng Li, Fang-Wei Wang |
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| Rok vydání: | 2006 |
| Předmět: |
Inclusion Bodies
Protein Folding Arginine Chemistry Protein Conformation Protein Renaturation Alpha interferon Interferon-alpha Recombinant Proteins law.invention Protein structure Biochemistry Protein refolding law Yield (chemistry) Interferon Type I Recombinant DNA Protein folding Protein Structure Quaternary Recombinant Consensus Interferon Biotechnology |
| Zdroj: | Protein expression and purification. 51(2) |
| ISSN: | 1046-5928 |
| Popis: | Arginine has been demonstrated to be capable of suppressing aggregation during protein refolding. However, the pathway and the mechanism for arginine to participate in and to assist refolding process still remains unclear. In this study, arginine-assisted refolding of recombinant consensus interferon (rIFN-con(1)) was investigated. It was found that although arginine minimized the formation of protein precipitate, it failed to prevent the formation of the soluble oligomeric species. The amount of the oligomers increased with the increase in arginine concentration. This phenomenon has not been reported. On the other hand, arginine was able to promote the yield of correctly refolded rIFN-con(1), which was more than 2 times higher than that in the absence of arginine. A proposed mechanism is the stabilization of different soluble species by arginine, which slowed down the conformational movement. The stabilization effect on native-like structure formation overwhelmed the oligomeric promotion effect, which resulted in a composite effect of increased refolding yield for rIFN-con, when arginine concentration was below 0.5 M. (c) 2006 Elsevier Inc. All rights reserved. |
| Databáze: | OpenAIRE |
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