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Design of Protein–Peptide Interaction Modules for Assembling Supramolecular Structures in Vivo and in Vitro
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)–pept...
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Published in: | ACS chemical biology 2015-09, Vol.10 (9), p.2108-2115 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 1554-8929 1554-8937 |
DOI: | 10.1021/acschembio.5b00415 |