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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
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Phage display of a catalytic antibody to optimize affinity for transition-state analog binding

机译:噬菌体展示催化抗体,以优化对过渡态类似物结合的亲和力

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摘要

Catalytic antibodies have shown great prom- ise for catalyzing a tremendously diverse set of natural and unnatural chemical transformations. However, few catalytic antibodies have efficiencies that approach those of natural enzymes. In principle, random mutagenesis procedures such as phage display could be used to improve the catalytic activities of existing antibodies; however, these studies have been hampered by difficulties in the recombinant expression of antibodies. Here, we have grafted the antigen binding loops from a murine-derived catalytic antibody, 17E8, onto a human antibody framework in an effort to overcome difficulties associated with recombinant expression and phage display of this antibody.
机译:催化抗体已显示出极大的潜力,可催化多种多样的自然和非自然化学转化。然而,几乎没有催化抗体具有接近天然酶的效率。原则上,可以使用随机诱变程序(例如噬菌体展示)来提高现有抗体的催化活性。然而,这些研究由于抗体的重组表达困难而受到阻碍。在这里,我们已经将鼠源催化抗体17E8的抗原结合环移植到人抗体框架上,以克服与该抗体的重组表达和噬菌体展示相关的困难。

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