Peptide–oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic

Chenguang Lou, Manuel C. Martos-Maldonado, Charlotte S. Madsen, Rasmus P. Thomsen, Søren Roi Midtgaard, Niels Johan Christensen, Jørgen Kjems, Peter W. Thulstrup, Jesper Wengel () and Knud J. Jensen ()
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Chenguang Lou: Chemistry and Pharmacy, Biomolecular Nanoscale Engineering Center, University of Southern Denmark
Manuel C. Martos-Maldonado: Biomolecular Nanoscale Engineering Center, University of Copenhagen
Charlotte S. Madsen: Biomolecular Nanoscale Engineering Center, University of Copenhagen
Rasmus P. Thomsen: Biomolecular Nanoscale Engineering Center and Interdisciplinary Nanoscience Center (iNANO), University of Aarhus
Søren Roi Midtgaard: Niels Bohr Institute, University of Copenhagen
Niels Johan Christensen: Biomolecular Nanoscale Engineering Center, University of Copenhagen
Jørgen Kjems: Biomolecular Nanoscale Engineering Center and Interdisciplinary Nanoscience Center (iNANO), University of Aarhus
Peter W. Thulstrup: University of Copenhagen
Jesper Wengel: Chemistry and Pharmacy, Biomolecular Nanoscale Engineering Center, University of Southern Denmark
Knud J. Jensen: Biomolecular Nanoscale Engineering Center, University of Copenhagen

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Peptide-based structures can be designed to yield artificial proteins with specific folding patterns and functions. Template-based assembly of peptide units is one design option, but the use of two orthogonal self-assembly principles, oligonucleotide triple helix and a coiled coil protein domain formation have never been realized for de novo protein design. Here, we show the applicability of peptide–oligonucleotide conjugates for self-assembly of higher-ordered protein-like structures. The resulting nano-assemblies were characterized by ultraviolet-melting, gel electrophoresis, circular dichroism (CD) spectroscopy, small-angle X-ray scattering and transmission electron microscopy. These studies revealed the formation of the desired triple helix and coiled coil domains at low concentrations, while a dimer of trimers was dominating at high concentration. CD spectroscopy showed an extraordinarily high degree of α-helicity for the peptide moieties in the assemblies. The results validate the use of orthogonal self-assembly principles as a paradigm for de novo protein design.

Date: 2016
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DOI: 10.1038/ncomms12294

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