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Small-Molecule-Triggered and Light-Controlled Reversible Regulation of Enzymatic Activity

The fine control of enzyme activity is essential for the regulation of many important cellular and organismal functions. The light-regulation of proteins serves as an important method for the spatiotemporal control over the production and degradation of an enzyme product. This area is of intense int... Full description

Journal Title: Journal of the American Chemical Society 27 January 2016, Vol.138(3), pp.955-61
Main Author: Tian, Tian
Other Authors: Song, Yanyan , Wang, Jiaqi , Fu, Boshi , He, Zhiyong , Xu, Xianqun , Li, Anling , Zhou, Xin , Wang, Shaoru , Zhou, Xiang
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; PMID: 26741151 Version:1 ; DOI: 10.1021/jacs.5b11532
Link: http://pubmed.gov/26741151
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recordid: medline26741151
title: Small-Molecule-Triggered and Light-Controlled Reversible Regulation of Enzymatic Activity
format: Article
creator:
  • Tian, Tian
  • Song, Yanyan
  • Wang, Jiaqi
  • Fu, Boshi
  • He, Zhiyong
  • Xu, Xianqun
  • Li, Anling
  • Zhou, Xin
  • Wang, Shaoru
  • Zhou, Xiang
subjects:
  • Light
  • Small Molecule Libraries -- Pharmacology
  • Thrombin -- Antagonists & Inhibitors
ispartof: Journal of the American Chemical Society, 27 January 2016, Vol.138(3), pp.955-61
description: The fine control of enzyme activity is essential for the regulation of many important cellular and organismal functions. The light-regulation of proteins serves as an important method for the spatiotemporal control over the production and degradation of an enzyme product. This area is of intense interest for researchers. To the best of our knowledge, the use of small molecules as light-triggered molecular switches to reversibly control enzyme activity at the protein level has not yet been studied. In the present study, we demonstrate the light-controlled reversible regulation of the enzyme using a small-molecule-triggered switch, which is based on molecular recognition between an azobenzene derivative and telomere DNA. This molecule interconverts between the trans and cis states under alternate 365 nm UV and visible light irradiation, which consequently triggers the compaction and extension of telomere DNA. We further provide direct evidence for this structural switch using a circular dichroism study. Furthermore, our strategy has been successfully used to effectively control blood clotting in human plasma.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; PMID: 26741151 Version:1 ; DOI: 10.1021/jacs.5b11532
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleSmall-Molecule-Triggered and Light-Controlled Reversible Regulation of Enzymatic Activity
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subjectLight ; Small Molecule Libraries -- Pharmacology ; Thrombin -- Antagonists & Inhibitors
descriptionThe fine control of enzyme activity is essential for the regulation of many important cellular and organismal functions. The light-regulation of proteins serves as an important method for the spatiotemporal control over the production and degradation of an enzyme product. This area is of intense interest for researchers. To the best of our knowledge, the use of small molecules as light-triggered molecular switches to reversibly control enzyme activity at the protein level has not yet been studied. In the present study, we demonstrate the light-controlled reversible regulation of the enzyme using a small-molecule-triggered switch, which is based on molecular recognition between an azobenzene derivative and telomere DNA. This molecule interconverts between the trans and cis states under alternate 365 nm UV and visible light irradiation, which consequently triggers the compaction and extension of telomere DNA. We further provide direct evidence for this structural switch using a circular dichroism study. Furthermore, our strategy has been successfully used to effectively control blood clotting in human plasma.
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abstractThe fine control of enzyme activity is essential for the regulation of many important cellular and organismal functions. The light-regulation of proteins serves as an important method for the spatiotemporal control over the production and degradation of an enzyme product. This area is of intense interest for researchers. To the best of our knowledge, the use of small molecules as light-triggered molecular switches to reversibly control enzyme activity at the protein level has not yet been studied. In the present study, we demonstrate the light-controlled reversible regulation of the enzyme using a small-molecule-triggered switch, which is based on molecular recognition between an azobenzene derivative and telomere DNA. This molecule interconverts between the trans and cis states under alternate 365 nm UV and visible light irradiation, which consequently triggers the compaction and extension of telomere DNA. We further provide direct evidence for this structural switch using a circular dichroism study. Furthermore, our strategy has been successfully used to effectively control blood clotting in human plasma.
doi10.1021/jacs.5b11532
pmid26741151
issn00027863
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date2016-01-27