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首页> 外文期刊>Antibodies >Refolding Technology for scFv Using a New Detergent, N-Lauroyl-L-glutamate and Arginine
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Refolding Technology for scFv Using a New Detergent, N-Lauroyl-L-glutamate and Arginine

机译：使用新型洗涤剂，N-月桂酰-L-谷氨酸和精氨酸的scFv折叠技术

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Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding sites, is extensively investigated. It becomes increasingly apparent, however, that these smaller fragments of antibodies are rather difficult to produce, as the normally efficient mammalian secretion system does not work well for these fragments. Thus, refolding of insoluble proteins produced in Escherichia coli is a method of choice, although such refolding is mainly based on trial-and-error experiment. Here we describe a novel refolding system using a new amino acid-based detergent, N-lauroyl-L-glutamate, and arginine. This detergent appears to readily dissociate from proteins below critical micelle concentration (CMC), while remaining effective in protein solubilization above CMC. Arginine suppresses protein aggregation when the detergent concentration was reduced below CMC. The interaction of the detergent and arginine with proteins, which play an important role in protein refolding, will be discussed in great length.
机译：可溶性抗原或细胞表面标志物的单克隆抗体作为有效的人类疗法具有广阔的前景。主要缺点之一是其大尺寸，这阻止了有效地渗透到靶组织中。广泛研究了只有抗原结合位点的小分子抗体。然而，变得越来越明显的是，这些较小的抗体片段相当难以生产，因为通常有效的哺乳动物分泌系统不适用于这些片段。因此，重折叠在大肠杆菌中产生的不溶蛋白是一种选择的方法，尽管这种重折叠主要基于反复试验。在这里，我们描述了一种使用新的基于氨基酸的去污剂，N-月桂酰-L-谷氨酸和精氨酸的新型折叠系统。该去污剂似乎很容易从临界胶束浓度（CMC）以下的蛋白质上解离，而对CMC以上的蛋白质溶解仍然有效。当去污剂浓度降至CMC以下时，精氨酸可抑制蛋白质聚集。洗涤剂和精氨酸与蛋白质的相互作用将在蛋白质复性中发挥重要作用，将对此进行详尽的讨论。

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