ArticleJournal of the American Chemical Society2014
A set of computationally designed orthogonal antiparallel homodimers that expands the synthetic coiled-coil toolkit.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed.
- InsiliCoil: An Integrated Software Suite for Coiled Coil Design, Prediction, and Therapeutic Engineering.ACS synthetic biology · 2026Article
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- Beyond Dimerization: Harnessing Tetrameric Coiled-Coils for Nanostructure Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Exchange, promiscuity, and orthogonality inChemical science · 2025Article
- Coiled Coil Peptide Tiles (CCPTs): Expanding the Peptide Building Block Design with Multivalent Peptide Macrocycles.Journal of the American Chemical Society · 2024Article
- From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles.Chemical science · 2022Article
- De novo designed peptides for cellular delivery and subcellular localisation.Nature chemical biology · 2022Article
- Liposome fusion with orthogonal coiled coil peptides as fusogens: the efficacy of roleplaying peptides.Chemical science · 2021Article
- A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- DE-STRESS: a user-friendly web application for the evaluation of protein designs.Protein engineering, design & selection : PEDS · 2021Article
- Designed folding pathway of modular coiled-coil-based proteins.Nature communications · 2021Article
- Article
- Coiled-Coils: the Molecular Zippers that Self-Assemble Protein Nanostructures.International journal of molecular sciences · 2020Review
- Article
- Peptide design by optimization on a data-parameterized protein interaction landscape.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo.Nature biotechnology · 2017Article
- Modular assembly of a protein nanotriangle using orthogonally interacting coiled coils.Scientific reports · 2017Article
- Coassembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Journal of the American Chemical Society · 2016Article
- Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Journal of the American Chemical Society · 2016Article
- Flexible, symmetry-directed approach to assembling protein cages.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Molecular engineering of protein assemblies, including the fabrication of nanostructures and synthetic signaling pathways, relies on the availability of modular parts that can be combined to give different structures and functions. Currently, a limited number of well-characterized protein interaction components are available. Coiled-coil interaction modules have been demonstrated to be useful for biomolecular design, and many parallel homodimers and heterodimers are available in the coiled-coil toolkit. In this work, we sought to design a set of orthogonal antiparallel homodimeric coiled coils using a computational approach. There are very few antiparallel homodimers described in the literature, and none have been measured for cross-reactivity. We tested the ability of the distance-dependent statistical potential DFIRE to predict orientation preferences for coiled-coil dimers of known structure. The DFIRE model was then combined with the CLASSY multistate protein design framework to engineer sets of three orthogonal antiparallel homodimeric coiled coils. Experimental measurements confirmed the successful design of three peptides that preferentially formed antiparallel homodimers that, furthermore, did not interact with one additional previously reported antiparallel homodimer. Two designed peptides that formed higher-order structures suggest how future design protocols could be improved. The successful designs represent a significant expansion of the existing protein-interaction toolbox for molecular engineers.
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