Campus Units

Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

5-2011

Journal or Book Title

Journal of the American Chemical Society

Volume

133

Issue

23

First Page

8862

Last Page

8865

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

Included in

Chemistry Commons

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