New designed protein assemblies

Curr Opin Chem Biol. 2013 Dec;17(6):940-5. doi: 10.1016/j.cbpa.2013.10.014. Epub 2013 Oct 31.


Self-assembly is an essential concept of all organisms. Polypeptides self-assemble either within a single polypeptide chain or through assembly of protein domains. Recent advances in designed protein assemblies were achieved by genetic or chemical linkage of oligomerization domains and by engineering new interaction interfaces, which resulted in formation of lattices and cage-like protein assemblies. The absence of new experimentally determined protein folds in the last few years underlines the challenge of designing new folds. Recently a new strategy for designing self-assembly of a polypeptide fold, based on the topological arrangement of coiled-coil modules as the protein origami, has been proposed. The polypeptide tetrahedron was designed from a single chain concatenating of coiled-coil forming building modules interspersed with flexible hinges. In this strategy the order of coiled-coil segments defines the fold of the polypeptide nanostructure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Models, Molecular
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Multimerization*
  • Proteins / chemistry*
  • Proteins / metabolism


  • Peptides
  • Proteins