In:
Angewandte Chemie International Edition, Wiley, Vol. 57, No. 24 ( 2018-06-11), p. 7126-7130
Kurzfassung:
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.
Materialart:
Online-Ressource
ISSN:
1433-7851
,
1521-3773
DOI:
10.1002/anie.201803232
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2018
ZDB Id:
2011836-3
ZDB Id:
123227-7
