Jump to main content
Jump to site search


Exploring cucurbit[6]uril-peptide interactions in the solid state: crystal structure of cucurbit[6]uril complexes with glycyl-containing dipeptides

Abstract

Macrocyclic host cucurbit[6]uril forms supramolecular complexes with dipeptides sequenced as Gly-X (X is either an aromatic amino acid residue Phe, Tyr, Trp or Gly) in the solid state. Despite exclusion complexation, the interaction between guest dipeptide and host cucurbit[6]uril is multipoint in the solid state. The ammonium and amide nitrogen atoms of dipeptide participate in ion-dipole and hydrogen bonding with host carbonyl rim and water molecules (or chloride anion) trapped inside the macrocyclic cavity. The structural study reveales the stabilizing role of the aromatic residues on the supramolecular assembly due to their complementarity with the outer surface of cucurbit[6]uril. In the absence of aromatic side chain the calcium ion can stabilize and guide the supramolecular assembly between macrocycle and Gly-Gly dipeptide.

Back to tab navigation

Supplementary files

Publication details

The article was received on 09 May 2017, accepted on 14 Jun 2017 and first published on 15 Jun 2017


Article type: Communication
DOI: 10.1039/C7CE00881C
Citation: CrystEngComm, 2017, Accepted Manuscript
  •   Request permissions

    Exploring cucurbit[6]uril-peptide interactions in the solid state: crystal structure of cucurbit[6]uril complexes with glycyl-containing dipeptides

    O. Danylyuk, CrystEngComm, 2017, Accepted Manuscript , DOI: 10.1039/C7CE00881C

Search articles by author

Spotlight

Advertisements