De Novo Designed α-Helical Coiled-Coil Peptides as Scaffolds for Chemical Reactions

被引:23
作者
Rink, W. Mathis [1 ]
Thomas, Franziska [1 ,2 ]
机构
[1] Georg August Univ Gottingen, Inst Organ & Biomol Chem, Tammannstr 2, D-37077 Gottingen, Germany
[2] Ctr Biostruct Imaging Neurodegenerat, Von Siebold Str 3a, D-37075 Gottingen, Germany
关键词
coiled coil; de novo design; enzyme; proximity-induced reactions; reaction scaffold; INTERHELICAL SALT BRIDGES; SELF-REPLICATION; MEMBRANE-PROTEINS; CRYSTAL-STRUCTURE; BIOMIMETIC CATALYSIS; STRAND DISPLACEMENT; PROBE SYSTEM; STABILITY; SITE; BINDING;
D O I
10.1002/chem.201802849
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Coiled coils (CCs) are well-understood protein-folding motifs. They appear in a variety of oligomer states and as homo- and heteromeric assemblies. This versatility and the general accessibility by de novo design makes them ideal building blocks for synthetic biology. This Minireview highlights the efforts being made in designing small peptide catalysts or reaction templates based on the CC scaffold. The first reports described autocatalysis or mediation of peptide ligation based on CC recognition. Over the years, the designs became more advanced, catalyzing ester hydrolysis, acyl transfer and redox reactions with partial enzyme-like reactivity. Due to the ability to control CC assembly, and, in heterodimeric systems, the association and dissociation, the CC motif has become a common peptide tag in chemical biology.
引用
收藏
页码:1665 / 1677
页数:13
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