A Designed Non-Peptidic Receptor that Mimics the Phosphocholine Binding Site of the McPC603 Antibody

A Designed Non-Peptidic Receptor that Mimics the Phosphocholine Binding Site of the McPC603 Antibody

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 rig...

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Veröffentlicht in:Angewandte Chemie International Edition 1996-08, Vol.35 (15), p.1712-1715
Hauptverfasser: Magrans, J. Oriol, Ortiz, Angel R., Molins, M. Antònia, Lebouille, Paul H. P., Sánchez-Quesada, Jorge, Prados, Pilar, Pons, Miquel, Gago, Federico, de Mendoza, Javier
Format: Artikel
Sprache:eng
Schlagworte:
calixarenes
molecular dynamics simulations
molecular recognition
phospholipids
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Beschreibung
Zusammenfassung: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.
ISSN:0570-0833
1521-3773
DOI:10.1002/anie.199617121