title: Beta-peptide bundles with fluorous cores.
abstract: We reported recently that certain beta-peptides self-assemble spontaneously into cooperatively folded bundles whose kinetic and thermodynamic metrics mirror those of natural helix bundle proteins. The structures of four such beta-peptide bundles are known in atomic detail. These structures reveal a solvent-sequestered, hydrophobic core stabilized by a unique arrangement of leucine side chains and backbone methylene groups. Here we report that this hydrophobic core can be re-engineered to contain a fluorous subdomain while maintaining the characteristic beta-peptide bundle fold. Like alpha-helical bundles possessing fluorous cores, fluorous beta-peptide bundles are stabilized relative to hydrocarbon analogues and undergo cold denaturation. Beta-peptide bundles with fluorous cores represent the essential first step in the synthesis of orthogonal protein assemblies that can sequester selectively in an interstitial membrane environment.
authors.affiliation: Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Molski
authors.forename: Jessica L
authors.initials: JL
authors.lastname: Goodman
authors.forename: Cody J
authors.initials: CJ
authors.lastname: Craig
authors.forename: He
authors.initials: H
authors.lastname: Meng
authors.forename: Krishna
authors.initials: K
authors.lastname: Kumar
authors.forename: Alanna
authors.initials: A
authors.lastname: Schepartz
mesh_terms: D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D007700:Kinetics; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
chemical_list: D010455:Peptides