Cucurbit[7]uril-Dimethyllysine Recognition in a Model Protein.

Cucurbit[7]uril-Dimethyllysine Recognition in a Model Protein.
Angew Chem Int Ed Engl. 2018 Apr 19;:
Authors: Guagnini F, Antonik P, Rennie M, O'Byrne P, Khan A, Pinalli R, Dalcanale E, Crowley PB
Abstract
Here, we provide the first structural characterization of host-guest complexation between cucurbit[7]uril (Q7) and dimethyl-lysine (KMe2) 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-KMe2 complexation were revealed by X-ray crystallography. The crystal structures revealed also entrapped water molecules that persisted in solvating 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.
PMID: 29673020 [PubMed - as supplied by publisher]

Source: Angewandte Chemie - April 19, 2018 Category: Chemistry Authors: Guagnini F, Antonik P, Rennie M, O'Byrne P, Khan A, Pinalli R, Dalcanale E, Crowley PB Tags: Angew Chem Int Ed Engl Source Type: research