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ACS Chem Biol. 2015 Sep 18;10(9):2108-15. doi: 10.1021/acschembio.5b00415. Epub 2015 Jul 17.

Design of Protein-Peptide Interaction Modules for Assembling Supramolecular Structures in Vivo and in Vitro.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University , New Haven, Connecticut 06511, United States.
2
Department of Chemistry, Yale University , New Haven, Connecticut 06511, United States.
3
Integrated Graduate Program in Physical and Engineering Biology , New Haven, Connecticut 06511, United States.

Abstract

Synthetic biology and protein origami both require protein building blocks that behave in a reliable, predictable fashion. In particular, we require protein interaction modules with known specificity and affinity. Here, we describe three designed TRAP (Tetratricopeptide Repeat Affinity Protein)-peptide interaction pairs that are functional in vivo. We show that each TRAP binds to its cognate peptide and exhibits low cross-reactivity with the peptides bound by the other TRAPs. In addition, we demonstrate that the TRAP-peptide interactions are functional in many cellular contexts. In extensions of these designs, we show that the binding affinity of a TRAP-peptide pair can be systematically varied. The TRAP-peptide pairs we present thus represent a powerful set of new building blocks that are suitable for a variety of applications.

PMID:
26131725
DOI:
10.1021/acschembio.5b00415
[Indexed for MEDLINE]

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