Design of protein-peptide interaction modules for assembling supramolecular structures in vivo and in vitro

Elizabeth B Speltz, Aparna Nathan, Lynne Regan

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)2108-2115
Number of pages8
JournalAcs chemical biology
Volume10
Issue number9
Early online date17 Jul 2015
DOIs
Publication statusPublished - 18 Sep 2015

Keywords

  • 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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