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• W2000481567 abstract "We reported recently that certain β-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 β-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 β-peptide bundle fold. Like α-helical bundles possessing fluorous cores, fluorous β-peptide bundles are stabilized relative to hydrocarbon analogues and undergo cold denaturation. β-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." @default.
• W2000481567 created "2016-06-24" @default.
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• W2000481567 date "2010-03-02" @default.
• W2000481567 modified "2023-10-11" @default.
• W2000481567 title "β-Peptide Bundles with Fluorous Cores" @default.
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• W2000481567 doi "https://doi.org/10.1021/ja910903c" @default.
• W2000481567 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2842013" @default.
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