Triangular prism-shaped β-peptoid helices as unique biomimetic scaffolds
| Autor: | Jonas S. Laursen, Christian A. Olsen, Peter Fristrup, Pernille Harris |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Protein Folding
Circular dichroism Materials science Chemical biology General Physics and Astronomy Crystal structure Molecular Dynamics Simulation Crystallography X-Ray Article Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Peptoids Structure-Activity Relationship chemistry.chemical_compound Molecular dynamics Isomerism Biomimetic Materials Structure–activity relationship Multidisciplinary Tissue Scaffolds Circular Dichroism Peptoid General Chemistry Crystallography Spectrometry Fluorescence Chemical sciences chemistry Drug Design Protein folding Triangular prism Protein Multimerization |
| Zdroj: | Nature Communications Laursen, J S, Harris, P, Fristrup, P & Olsen, C A 2015, ' Triangular prism-shaped β-peptoid helices as unique biomimetic scaffolds ', Nature Communications, vol. 6, 7013 . https://doi.org/10.1038/ncomms8013 |
| ISSN: | 2041-1723 |
| Popis: | β-Peptoids are peptidomimetics based on N-alkylated β-aminopropionic acid residues (or N-alkyl-β-alanines). This type of peptide mimic has previously been incorporated in biologically active ligands and has been hypothesized to be able to exhibit foldamer properties. Here we show, for the first time, that β-peptoids can be tuned to fold into stable helical structures. We provide high-resolution X-ray crystal structures of homomeric β-peptoid hexamers, which reveal right-handed helical conformations with exactly three residues per turn and a helical pitch of 9.6–9.8 Å between turns. The presence of folded conformations in solution is supported by circular dichroism spectroscopy showing length- and solvent dependency, and molecular dynamics simulations provide further support for a stabilized helical secondary structure in organic solvent. We thus outline a framework for future design of novel biomimetics that display functional groups with high accuracy in three dimensions, which has potential for development of new functional materials. β-Peptoids are based on N-alkylated β-aminopropionic acid residues, which have been inspired by the more intensely studied peptoids and β-peptides. Here, the authors report X-ray crystal structures of oligomeric β-peptoids demonstrating secondary structures with this backbone. |
| Databáze: | OpenAIRE |
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