Altered binding of a multimeric protein by changing the self-assembling properties of its substrate.

Artificially controlled cell recognition has potentially far-reaching applications in both the understanding and altering of biological function. The event of recognition often involves a multimeric protein binding a cellular membrane. While such an interaction is energetically favorable, it has been surprisingly underexploited in artificial control of recognition.

Self-assembly of a four-helix bundle on a DNA quadruplex.

Come together: A novel method for assembling monomers and controlling structure of a de novo helix bundle protein is described. A guanine (G)-rich oligodeoxynucleotide scaffold forms a hydrogen-bonded DNA quadruplex in the presence of potassium counterions, thereby inducing a helical structure and fourfold stoichiometry in conjugated, amphiphilic peptide sequences. The DNA scaffold shows potential for rapidly assembling designed proteins.

Multivalent protein binding and precipitation by self-assembling molecules on a DNA pentaplex scaffold.

A supramolecular assembly containing an isoguanosine pentaplex with both a "protein-binding" face and a "reporter" face has been generated. When phosphocholine is appended to the protein-binding face this supramolecular assembly binds multivalently to the pentameric human C-reactive protein, a biomolecule implicated in inflammation and heart disease.