Adaptive assembly: maximizing the potential of a given functional peptide with a tailor-made protein scaffold
Adaptive assembly: maximizing the potential of a given functional peptide with a tailor-made protein scaffold
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适应性组装：通过定制的蛋白质支架最大限度地发挥给定功能肽的潜力
DOI：
10.1016/j.chembiol.2015.07.015
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发表时间：
2015
影响因子：
--
通讯作者：
Honda S
中科院分区：
文献类型：
--
作者：
Watanabe H;Honda S
Protein engineering that exploits known functional peptides holds great promise for generating novel functional proteins. Here we propose a combinatorial approach, termed adaptive assembly, which provides a tailor-made protein scaffold for a given functional peptide. A combinatorial library was designed to create a tailor-made scaffold, which was generated from β hairpins derived from a 10-residue minimal protein "chignolin" and randomized amino acid sequences. We applied adaptive assembly to a peptide with low affinity for the Fc region of human immunoglobulin G, generating a 54-residue protein AF.p17 with a 40,600-fold enhanced affinity. The crystal structure of AF.p17 complexed with the Fc region revealed that the scaffold fixed the active conformation with a unique structure composed of a short α helix, β hairpins, and a loop-like structure. Adaptive assembly can take full advantage of known peptides as assets for generating novel functional proteins.
