AI Article Synopsis

  • Researchers can design artificial proteins by using peptide-based structures with specific folding and functions.
  • The study introduces a novel approach by combining oligonucleotide triple helix and coiled coil formation for self-assembly, demonstrating it can create higher-ordered protein-like structures.
  • Characterization techniques confirmed successful formation of the desired structures, showing significant stability and high α-helicity in the peptide assemblies, thus supporting the use of these self-assembly methods in protein design.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4974474PMC
http://dx.doi.org/10.1038/ncomms12294DOI Listing

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