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Cucurbit[7]uril‐Dimethyllysine Recognition in a Model Protein
Author(s) -
Guagnini Francesca,
Antonik Paweł M.,
Rennie Martin L.,
O'Byrne Peter,
Khan Amir R.,
Pinalli Roberta,
Dalcanale Enrico,
Crowley Peter B.
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201803232
Subject(s) - cucurbituril , steric effects , chemistry , molecule , octahedron , crystallography , selectivity , solid state , crystal structure , ammonium , stereochemistry , supramolecular chemistry , organic chemistry , catalysis
Here, we provide the first structural characterization of host–guest complexation between cucurbit[7]uril ( Q7 ) and dimethyllysine (KMe 2 ) in a model protein. Binding was dominated by complete encapsulation of the dimethylammonium functional group. While selectivity for the most sterically accessible dimethyllysine was observed both in solution and in the solid state, three different modes of Q7 ‐KMe 2 complexation were revealed by X‐ray crystallography. The crystal structures revealed also entrapped water molecules that solvated the ammonium group within the Q7 cavity. Remarkable Q7 ‐protein assemblies, including inter‐locked octahedral cages that comprise 24 protein trimers, occurred in the solid state. Cucurbituril clusters appear to be responsible for these assemblies, suggesting a strategy to generate controlled protein architectures.