Expanding the chemical diversity of M13 bacteriophage.

Expanding the chemical diversity of M13 bacteriophage.
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DOI:
10.3389/fmicb.2022.961093
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发表时间:
2022
影响因子:
5.2
通讯作者:
--
中科院分区:
生物学2区
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噬菌体M13病毒粒子是非常稳定的纳米粒子,可以通过化学和遗传方法进行修饰。衣壳蛋白可以在各种化学反应中被功能化而不损失颗粒完整性。此外,遗传密码扩展(GCE)允许将非规范氨基酸(ncaa)引入显示的肽和蛋白质中。将ncAAs整合到噬菌体文库中,发现了具有低纳摩尔解离常数(KD)值的高亲和力结合物,可以潜在地用作抑制剂。本文综述了翻译过程中生物偶联和ncAAs的结合如何扩展了M13病毒粒子为各种目的所显示的肽和蛋白质的化学性质。
Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (KD) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.
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