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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Detalles Bibliográficos
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:
Chemistry
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
Descripción
Sumario: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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