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De Novo Designed α‐Helical Coiled‐Coil Peptides as Scaffolds for Chemical Reactions
Author(s) -
Rink W. Mathis,
Thomas Franziska
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201802849
Subject(s) - coiled coil , template , peptide , combinatorial chemistry , protein design , chemistry , linker , protein engineering , synthetic biology , autocatalysis , biochemistry , nanotechnology , protein structure , computational biology , enzyme , biology , materials science , computer science , catalysis , operating system
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.