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Issue 3, 2016
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Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen–antibody interactions

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Abstract

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-K96NPE, 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-K96NPE was demonstrated as a proof of concept to quantify B cell synapse formation and calcium influx responses at the single cell level.

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

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Publication details

The article was received on 10 Sep 2015, accepted on 19 Nov 2015 and first published on 11 Dec 2015


Article type: Edge Article
DOI: 10.1039/C5SC03404C
Chem. Sci., 2016,7, 1891-1895
  • Open access: Creative Commons BY license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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

    S. Tang, Z. Wan, Y. Gao, J. Zheng, J. Wang, Y. Si, X. Chen, H. Qi, L. Liu and W. Liu, Chem. Sci., 2016, 7, 1891
    DOI: 10.1039/C5SC03404C

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