Cross‐Linked Micelles with Enzyme‐Like Active Sites for Biomimetic Hydrolysis of Activated Esters

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2017-08-01
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Hu, Lan
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Zhao, Yan
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Chemistry

The Department of Chemistry seeks to provide students with a foundation in the fundamentals and application of chemical theories and processes of the lab. Thus prepared they me pursue careers as teachers, industry supervisors, or research chemists in a variety of domains (governmental, academic, etc).

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The Department of Chemistry was founded in 1880.

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Enzymes have substrate‐tailored active sites with optimized molecular recognition and catalytic features. Although many different platforms have been used by chemists to construct enzyme mimics, it is challenging to tune the structure of their active sites systematically. By molecularly imprinting template molecules within doubly cross‐linked micelles, we created protein‐sized nanoparticles with catalytically functionalized binding sites. These enzyme mimics accelerated the hydrolysis of activated esters thousands of times over the background reaction, whereas the analogous catalytic group (a nucleophilic pyridyl derivative) was completely inactive in bulk solution under the same conditions. The template molecules directly controlled the size and shape of the active site and modulated the resulting catalyst's performance at different pHs. The synthetic catalysts displayed Michaelis–Menten enzymatic behavior and, interestingly, reversed the intrinsic reactivity of the activated esters during the hydrolysis.

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This is the peer-reviewed version of the following article: Hu, Lan, and Yan Zhao. "Cross‐Linked Micelles with Enzyme‐Like Active Sites for Biomimetic Hydrolysis of Activated Esters." Helvetica Chimica Acta 100, no. 8 (2017): e1700147., which has been published in final form at DOI: 10.1002/hlca.201700147. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.

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Sun Jan 01 00:00:00 UTC 2017
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