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 |
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| container_title | Angewandte Chemie International Edition |
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| creator | 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 |
| description | 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. |
| doi_str_mv | 10.1002/anie.199617121 |
| format | Article |
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| recordid | cdi_crossref_primary_10_1002_anie_199617121 |
| source | Access via Wiley Online Library |
| subjects | calixarenes molecular dynamics simulations molecular recognition phospholipids |
| title | A Designed Non-Peptidic Receptor that Mimics the Phosphocholine Binding Site of the McPC603 Antibody |
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