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An Entropically Efficient Supramolecular Inhibition Strategy for Shiga Toxins
Author(s) -
Kitov Pavel I.,
Lipinski Tomasz,
Paszkiewicz Eugenia,
Solomon Dmitry,
Sadowska Joanna M.,
Grant Gordon A.,
Mulvey George L.,
Kitova Elena N.,
Klassen John S.,
Armstrong Glen D.,
Bundle David R.
Publication year - 2008
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.200704064
Subject(s) - linker , supramolecular chemistry , chemistry , ligand (biochemistry) , shiga toxin , toxin , microbial toxins , amyloid (mycology) , endogeny , combinatorial chemistry , biochemistry , escherichia coli , computer science , receptor , crystallography , inorganic chemistry , crystal structure , gene , operating system
A compact heterobifunctional ligand devoid of a linker between binding functionalities induces a supramolecular assembly between two pentameric proteins, Shiga toxin (blue) and serum amyloid P component, a human serum protein (turquoise). The use of an endogenous protein as a template brings about a 10 000‐fold enhancement of ligand activity.