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Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions† †Electronic supplementary information (ESI) available: Experimental section. See DOI: 10.1039/c5sc03404c

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. We report the chemical synthesis of the first photo-activatable protein antigen that can be used to study antigen–antibody interaction...

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Bibliographic Details
Published in:Chemical science (Cambridge) 2015-12, Vol.7 (3), p.1891-1895
Main Authors: Tang, Shan, Wan, Zhengpeng, Gao, Yiren, Zheng, Ji-Shen, Wang, Jing, Si, Yan-Yan, Chen, Xin, Qi, Hai, Liu, Lei, Liu, Wanli
Format: Article
Language:English
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Summary: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. 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.
ISSN:2041-6520
2041-6539
DOI:10.1039/c5sc03404c