Abstract / Description of output
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.
Original language | English |
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Pages (from-to) | 2108-2115 |
Number of pages | 8 |
Journal | Acs chemical biology |
Volume | 10 |
Issue number | 9 |
Early online date | 17 Jul 2015 |
DOIs | |
Publication status | Published - 18 Sept 2015 |
Keywords / Materials (for Non-textual outputs)
- amino acid sequence
- escherichia coli
- escherichia coli proteins
- HEK293 cells
- HSP90 heat-shock proteins
- HeLa cells
- homeodomain proteins
- humans
- models
- peptides
- protein interaction domains and motifs
- protein interaction maps
- proteins
- tumor suppressor proteins
- molecular
- genetics
- monomers
- assays
- chemical specificity
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Lynne Regan
- School of Biological Sciences - Chair of Interdisciplinary Science
- Centre for Engineering Biology
Person: Academic: Research Active