Premium
A Designed Non‐Peptidic Receptor that Mimics the Phosphocholine Binding Site of the McPC603 Antibody
Author(s) -
Magrans J. Oriol,
Ortiz Angel R.,
Molins M. Antònia,
Lebouille Paul H. P.,
SánchezQuesada Jorge,
Prados Pilar,
Pons Miquel,
Gago Federico,
de Mendoza Javier
Publication year - 1996
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199617121
Subject(s) - phosphorylcholine , chemistry , choline , phosphocholine , hydrogen bond , receptor , binding site , stereochemistry , antibody , biochemistry , molecule , phospholipid , organic chemistry , biology , phosphatidylcholine , membrane , immunology
The two key interactions in the binding of phosphorylcholine by the antibody McPC603 are utilized in the complexation of dioctanoyl‐ L ‐α‐phosphatidyl‐choline (DOPC) and a novel non‐peptidic abiotic receptor. These interactions are drawn as dotted lines in the structure of the complex shown on the right: hydrogen bonds between the choline phosphate and the guanidinium unit of the receptor, and cation–π interactions between the ammonium group of DOPC and the calixarene unit of the receptor.