Published December 14, 1990
| public
Journal Article
Acetylcholine Binding by a Synthetic Receptor: Implications for Biological Recognition
- Creators
-
Dougherty, Dennis A.
- Stauffer, David A.
Abstract
The neurotransmitter acetylcholine (ACh) is bound with 50-micromolar affinity by a completely synthetic receptor (host) comprising primarily aromatic rings. The host provided an overall hydrophobic binding site, but one that could recognize the positive charge of the quaternary ammonium group of ACh through a stabilizing interaction with the electron-rich π systems of the aromatic rings (cation-π interaction). Similar interactions may be involved in biological recognition of ACh and other choline derivatives.
Additional Information
© 1990 American Association for the Advancement of Science. Received 17 July 1990; accepted 11 September 1990. Supported by the Office of Naval Research (N000014-88-K-0259) and the National Institutes of Health (GM36356 and GM43936). We thank H. Lester and A. Karlin for helpful discussions and W. L. Jorgensen for providing a copy of the program BOSS. Contribution no. 8174 from the Division of Chemistry and Chemical Engineering, California Institute of Technology.Additional details
- Eprint ID
- 53621
- DOI
- 10.1126/science.2274786
- Resolver ID
- CaltechAUTHORS:20150113-105035358
- N000014-88-K-0259
- Office of Naval Research (ONR)
- GM36356
- NIH
- GM43936
- NIH
- Created
-
2015-01-13Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Division of Chemistry and Chemical Engineering
- Other Numbering System Identifier
- 8174