Journal article
Enhancing Binding Affinity by the Cooperativity between Host Conformation and Host-Guest Interactions
Journal of the American Chemical Society, Vol.133(23), pp.8862-8865
06/15/2011
DOI: 10.1021/ja203117g
PMID: 21574588
Abstract
Glutamate-functionalized oligocholate foldamers bound Zn(OAc)(2), guanidine, and even amine compounds with surprisingly high affinities. The conformational change of the hosts during binding was crucial to the enhanced binding affinity. The strongest cooperativity between the conformation and guest-binding occurred when the hosts were unfolded but near the folding-unfolding transition. These results suggest that high binding affinity in molecular recognition may be more easily obtained from large hosts capable of strong cooperative conformational changes instead of those with rigid, preorganized structures.
Details
- Title: Subtitle
- Enhancing Binding Affinity by the Cooperativity between Host Conformation and Host-Guest Interactions
- Creators
- Zhenqi Zhong - Iowa State UniversityXueshu Li - Iowa State UniversityYan Zhao - Iowa State University
- Resource Type
- Journal article
- Publication Details
- Journal of the American Chemical Society, Vol.133(23), pp.8862-8865
- Publisher
- Amer Chemical Soc
- DOI
- 10.1021/ja203117g
- PMID
- 21574588
- ISSN
- 0002-7863
- eISSN
- 1520-5126
- Number of pages
- 4
- Grant note
- DE-SC0002142 / U.S. Department of Energy, Office of Basic Energy Sciences; United States Department of Energy (DOE) 0946687 / Direct For Mathematical & Physical Scien; National Science Foundation (NSF); NSF - Directorate for Mathematical & Physical Sciences (MPS)
- Language
- English
- Date published
- 06/15/2011
- Academic Unit
- Occupational and Environmental Health
- Record Identifier
- 9984303284102771
Metrics
5 Record Views