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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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Published in: | Chemical science (Cambridge) 2015-12, Vol.7 (3), p.1891-1895 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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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
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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
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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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ISSN: | 2041-6520 2041-6539 |
DOI: | 10.1039/c5sc03404c |