Publication | Closed Access
Rational Design of Bioorganometallic Foldamers: A Potential Model for Parallel β‐Helical Peptides
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Citations
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References
2006
Year
EngineeringPeptide EngineeringMolecular BiologyPeptide ScienceProtein FoldingRational DesignRobust Model FoldamerBiophysicsParallel β‐Helical PeptidesProtein ChemistryBiochemistryFerrocene Amino AcidMolecular ModelingStructural BiologyBiomolecular EngineeringBioorganometallic FoldamersSelf-assemblyPeptide SynthesisMedicineNatural α-Amino Acid
Twists and turns: A series of alanine conjugates of ferrocene amino acid (Fca) were prepared based on the idea that an alternating sequence of a natural α-amino acid and a turn-inducing molecule may result in the formation of a robust model foldamer for β-helical peptides. Right- and left-handed pseudo-β-helical Fca–alanine foldamers were obtained, and their structures were studied in solution and the solid state. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2006/z602248_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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