Sharma G S, Singh L R
Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi, India.
Biochemistry (Mosc). 2017 Apr;82(4):465-473. doi: 10.1134/S0006297917040083.
Effects of solvent environments on protein refolding have gained significant attention due to their biotechnological and pharmaceutical applications. Recent advances have shown that a number of organic osmolytes have the unique ability to induce proper folding of several misfolded proteins and simultaneously inhibit aggregation during the process. In the present study, we investigated the effects of polyol osmolytes on the refolding of guanidinium chloride-denatured ribonuclease-A (RNase-A) and compared it with that of other osmolyte types. Measurements of enzymatic activity parameters (K and k) clearly indicate that polyol-induced RNase-A folding enhanced its catalytic efficiency as compared to folding in the absence of osmolytes or in the presence of osmolytes of other types. Furthermore, structural characterization revealed that the increase in catalytic efficiency stems from conformational alterations of the polyol-induced folded protein molecules as compared to other types of osmolytes.
由于其在生物技术和制药领域的应用，溶剂环境对蛋白质复性的影响已受到广泛关注。最近的研究进展表明，一些有机渗透剂具有独特的能力，能够诱导多种错误折叠的蛋白质正确折叠，并同时抑制该过程中的聚集现象。在本研究中，我们研究了多元醇渗透剂对氯化胍变性的核糖核酸酶 -A（RNase -A）复性的影响，并将其与其他类型的渗透剂进行了比较。酶活性参数（K和k）的测量清楚地表明，与在无渗透剂或存在其他类型渗透剂的情况下折叠相比，多元醇诱导的RNase -A折叠提高了其催化效率。此外，结构表征显示，与其他类型的渗透剂相比，催化效率的提高源于多元醇诱导的折叠蛋白分子的构象改变。
