Post-translational modification of genetically encoded polypeptide libraries

被引:27
作者
Angelini, Alessandro [1 ]
Heinis, Christian [1 ]
机构
[1] Ecole Polytech Fed Lausanne, Inst Chem Sci & Engn, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
MESSENGER-RNA DISPLAY; IN-VITRO SELECTION; PHAGE DISPLAY; CYCLIC-PEPTIDES; RIBOSOMAL SYNTHESIS; ANTIBODY LIBRARIES; PROTEIN EVOLUTION; LIGANDS; IDENTIFICATION; EPITOPE;
D O I
10.1016/j.cbpa.2011.03.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The genetic encoding of polypeptides with biological display systems enables the facile generation and screening of very large combinatorial libraries of molecules. By post-translationally modifying the encoded polypeptides, chemically and structurally more diverse molecules beyond linear amino acid polymers can be generated. The first post-translational modification applied to encoded polypeptides, the oxidation of cysteine residues to form disulfide bridges, is a natural one and was used to cyclise short peptides soon after the invention of phage display. Recently a range of non-natural chemical strategies for the post-translational modification of encoded polypeptide repertoires were applied to generate optical biosensors, semisynthetic polypeptides, peptide-drug conjugates, redox-insensitive monocyclic peptides or multicyclic peptides, and these strategies are reviewed in this article.
引用
收藏
页码:355 / 361
页数:7
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