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Multiplexed sorting of libraries on libraries: A novel method for empirical protein design by affinity-driven phage enrichment on synthetic peptide arrays

机译:文库的文库的多重排序:通过亲和力驱动的合成肽阵列上的噬菌体富集来进行经验性蛋白质设计的新方法

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摘要

Chemically synthesized peptide arrays on planar cellulose carriers are proposed as libraries of ligands suitable for the multiplexed simultaneous capture of peptide-specific acceptor proteins from a large randomly mutagenized library of acceptor proteins presented on bacteriophage M13 particles. This experimental set-up can be exploited to rapidly screen for individual new, distinct binding partners from two complementary libraries (two-dimensional screening). The technical feasibility of this empirical protein design approach was demonstrated with calmodulin as an aceptor protein using an array of mastoparan variants for multiplexed phage affinity enrichment.
机译:提出了在平面纤维素载体上化学合成的肽阵列作为适合于从噬菌体M13颗粒上随机诱变的大型受体蛋白文库中多重同时捕获肽特异性受体蛋白的配体库。可以利用该实验设置从两个互补库中快速筛选出各个新的,独特的结合伴侣(二维筛选)。使用钙调蛋白作为受体蛋白,并使用了一系列用于多聚体噬菌体亲和力富集的乳脂素变体,证明了这种经验蛋白设计方法的技术可行性。

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