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Protein Recognition by Functionalized Sulfonatocalix[4]arenes
Author(s) -
Doolan Aishling M.,
Rennie Martin L.,
Crowley Peter B.
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201704931
Subject(s) - ligand (biochemistry) , chemistry , dimer , calixarene , substituent , crystallography , porphyrin , crystal structure , stereochemistry , sulfonate , cytochrome , molecule , photochemistry , receptor , organic chemistry , sodium , biochemistry , enzyme
Abstract The interactions of two mono‐functionalized sulfonatocalix[4]arenes with cytochrome c were investigated by structural and thermodynamic methods. The replacement of a single sulfonate with either a bromo or a phenyl substituent resulted in altered recognition of cytochrome c as evidenced by X‐ray crystallography. The bromo‐substituted ligand yielded a new binding mode in which a self‐encapsulated calixarene dimer contributed to crystal packing. This ligand also formed a weak halogen bond with the protein. The phenyl‐substituted ligand was bound to Lys4 of cytochrome c, in a 1.7 Å resolution crystal structure. A dimeric packing arrangement mediated by ligand–ligand contacts in the crystal suggested a possible assembly mechanism. The different protein recognition properties of these calixarenes are discussed.