title: Positive allostery in metal ion binding by a cooperatively folded β-peptide bundle.
abstract: Metal ion binding is exploited by proteins in nature to catalyze reactions, bind molecules, and favor discrete structures, but it has not been demonstrated in β-peptides or their assemblies. Here we report the design, synthesis, and characterization of a β-peptide bundle that uniquely binds two Cd(II) ions in a distinct bicoordinate array. The two Cd(II) ions bind with positive allosteric cooperativity and increase the thermodynamic stability of the bundle by more than 50 °C. This system provides a unique, synthetic context to explore allosteric regulation and should pave the way to sophisticated molecular assemblies with catalytic and substrate-sensing functions that have historically not been available to de novo designed synthetic proteomimetics in water.
authors.affiliation: Department of Chemistry and ‡Department of Molecular, Cellular and Developmental Biology, Yale University , New Haven, Connecticut 06520-8107, United States.
authors.forename: Jonathan P
authors.initials: JP
authors.lastname: Miller
authors.forename: Michael S
authors.initials: MS
authors.lastname: Melicher
authors.forename: Alanna
authors.initials: A
authors.lastname: Schepartz
mesh_terms: D000494:Allosteric Regulation; D002104:Cadmium / Q000378:metabolism*; D015195:Drug Design; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D010455:Peptides; D002104:Cadmium