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Article
Enhancing Binding Affinity by the Cooperativity between Host Conformation and Host–Guest Interactions
Journal of the American Chemical Society
  • Zhenqi Zhong, Iowa State University
  • Xueshu Li, Iowa State University
  • Yan Zhao, Iowa State University
Document Type
Article
Disciplines
Publication Version
Published Version
Publication Date
5-1-2011
DOI
10.1021/ja203117g
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.
Comments

Reprinted (adapted) with permission from Journal of the American Chemical Society 133 (2011): 8862, doi:10.1021/ja203117g. Copyright 2011 American Chemical Society.

Copyright Owner
American Chemical Society
Language
en
File Format
application/pdf
Citation Information
Zhenqi Zhong, Xueshu Li and Yan Zhao. "Enhancing Binding Affinity by the Cooperativity between Host Conformation and Host–Guest Interactions" Journal of the American Chemical Society Vol. 133 Iss. 23 (2011) p. 8862 - 8865
Available at: http://works.bepress.com/yan_zhao/9/