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Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions

We report the chemical synthesis of the first photo-activatable protein antigen that can be used to study antigen–antibody interaction mediated responses in B cells. This strategy facilitated fine tuning of the caged protein antigen to optimize its bioactivity and photochemical properties. One optim...

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Autores principales: Tang, Shan, Wan, Zhengpeng, Gao, Yiren, Zheng, Ji-Shen, Wang, Jing, Si, Yan-Yan, Chen, Xin, Qi, Hai, Liu, Lei, Liu, Wanli
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5965250/
https://www.ncbi.nlm.nih.gov/pubmed/29899912
http://dx.doi.org/10.1039/c5sc03404c
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author Tang, Shan
Wan, Zhengpeng
Gao, Yiren
Zheng, Ji-Shen
Wang, Jing
Si, Yan-Yan
Chen, Xin
Qi, Hai
Liu, Lei
Liu, Wanli
author_facet Tang, Shan
Wan, Zhengpeng
Gao, Yiren
Zheng, Ji-Shen
Wang, Jing
Si, Yan-Yan
Chen, Xin
Qi, Hai
Liu, Lei
Liu, Wanli
author_sort Tang, Shan
collection PubMed
description We report the chemical synthesis of the first photo-activatable protein antigen that can be used to study antigen–antibody interaction mediated responses in B cells. This strategy facilitated fine tuning of the caged protein antigen to optimize its bioactivity and photochemical properties. One optimal molecule, HEL-K(96)NPE, was totally inert to hen egg lysozyme (HEL)-specific B cells and could only restore its antigenicity upon photoactivation. Combined with real time live cell imaging, the utility of HEL-K(96)NPE was demonstrated as a proof of concept to quantify B cell synapse formation and calcium influx responses at the single cell level.
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spelling pubmed-59652502018-06-13 Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions Tang, Shan Wan, Zhengpeng Gao, Yiren Zheng, Ji-Shen Wang, Jing Si, Yan-Yan Chen, Xin Qi, Hai Liu, Lei Liu, Wanli Chem Sci Chemistry We report the chemical synthesis of the first photo-activatable protein antigen that can be used to study antigen–antibody interaction mediated responses in B cells. This strategy facilitated fine tuning of the caged protein antigen to optimize its bioactivity and photochemical properties. One optimal molecule, HEL-K(96)NPE, was totally inert to hen egg lysozyme (HEL)-specific B cells and could only restore its antigenicity upon photoactivation. Combined with real time live cell imaging, the utility of HEL-K(96)NPE was demonstrated as a proof of concept to quantify B cell synapse formation and calcium influx responses at the single cell level. Royal Society of Chemistry 2016-03-01 2015-12-11 /pmc/articles/PMC5965250/ /pubmed/29899912 http://dx.doi.org/10.1039/c5sc03404c Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Tang, Shan
Wan, Zhengpeng
Gao, Yiren
Zheng, Ji-Shen
Wang, Jing
Si, Yan-Yan
Chen, Xin
Qi, Hai
Liu, Lei
Liu, Wanli
Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title_full Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title_fullStr Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title_full_unstemmed Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title_short Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
title_sort total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5965250/
https://www.ncbi.nlm.nih.gov/pubmed/29899912
http://dx.doi.org/10.1039/c5sc03404c
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