4.8 Article

Programmed Supramolecular Assemblies Using Orthogonal Pairs of Heterodimeric Coiled Coil Peptides

Journal

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 27, Pages -

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202201895

Keywords

alpha-Helices; Coiled Coils; Heterodimers; Nanostructures; Peptides; Supramolecular Assemblies

Funding

  1. National Science Foundation (NSF) [CHE-2002890]
  2. New York University Chemistry Department for the Margaret and Herman Sokol Fellowship
  3. NIH [R01AI108889]
  4. DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]

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Despite recent progress, it remains challenging to program biomacromolecules to assemble into discrete nanostructures with pre-determined sizes and topologies. Researchers have developed a novel strategy using two orthogonal pairs of heterodimeric coiled coils as building blocks to construct discrete supramolecular assemblies. These assemblies were characterized experimentally and showed good agreement with the designs, expanding the design paradigms for peptide-based discrete supramolecular assemblies and providing a route for de novo fabrication of functional protein materials.
Despite recent progress, it remains challenging to program biomacromolecules to assemble into discrete nanostructures with pre-determined sizes and topologies. We report here a novel strategy to address this challenge. By using two orthogonal pairs of heterodimeric coiled coils as the building blocks, we constructed six discrete supramolecular assemblies, each composed of a prescribed number of coiled coil components. Within these assemblies, different coiled coils were connected via end-to-side covalent linkages strategically pre-installed between the non-complementary pairs. The overall topological features of two highly complex assemblies, a barbell and a quadrilateral form, were characterized experimentally and were in good agreement to the designs. This work expands the design paradigms for peptide-based discrete supramolecular assemblies and will provide a route for de novo fabrication of functional protein materials.

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