Publication | Closed Access
Coordination‐Driven Folding and Assembly of a Short Peptide into a Protein‐like Two‐Nanometer‐Sized Channel
118
Citations
17
References
2014
Year
Supramolecular AssemblyProtein AssemblyPeptide EngineeringMolecular Self-assemblyMolecular BiologyPeptide ScienceChemistryShort Peptide HelicesProtein FoldingCoordination‐driven FoldingShort Peptide LigandBiophysicsShort PeptideMolecular MaterialProtein‐like Two‐nanometer‐sized ChannelNanodiscPeptide HelicesNanomaterialsNatural SciencesSelf-assemblyPeptide SynthesisProtein EngineeringMedicine
Short peptide helices have attracted attention as suitable building blocks for soft functional materials, but they are rarely seen in crystalline materials. A new artificial nanoassembly of short peptide helices in the crystalline state is presented in which peptide helices are arranged three-dimensionally by metal coordination. The folding and assembly processes of a short peptide ligand containing the Gly-Pro-Pro sequence were induced by silver(I) coordination in aqueous alcohol, and gave rise to a single crystal composed of polyproline II helices. Crystallographic studies revealed that this material possesses two types of unique helical nanochannel; the larger channel measures more than 2 nm in diameter. Guest uptake properties were investigated by soaking the crystals in polar solutions of guest molecules; anions, organic chiral molecules, and bio-oligomers are effectively encapsulated by this peptide-folded porous crystal, with moderate to high chiral recognition for chiral molecules.
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