关键词: antibody fragments bioconjugation combinatorial peptide libraries cross-linking cyclization peptide phage-display stop codon suppression

来  源:   DOI:10.3389/fmicb.2022.961093   PDF(Pubmed)

Abstract:
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 (K D) 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.
摘要:
噬菌体M13病毒粒子是非常稳定的纳米颗粒,可以通过化学和遗传方法进行修饰。衣壳蛋白可以在多种化学反应中官能化,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)引入展示的肽和蛋白质中。将ncAA掺入噬菌体文库已导致发现具有低纳摩尔解离常数(KD)值的高亲和力结合物,可潜在地用作抑制剂。本文回顾了翻译过程中ncAAs的生物缀合和掺入如何扩展了M13病毒体显示的肽和蛋白质的化学性质,用于各种目的。
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