Custom Membrane Proteins

 We have developed a practical procedure for expedient and cost-effective synthesis of small to medium-sized membrane proteins in multi-milligram scale through the use of automated Fmoc chemistry. After the attachment of a removable arginine-tagged backbone modification group, the membrane protein segments behave almost the same as ordinary water-soluble peptides in terms of Fmoc solid-phase synthesis, ligation, purification, and mass spectrometry characterization. The efficiency and practicality of the method is demonstrated by the successful preparation of Ser64-phosphorylated M2 proton channel from influenza A virus and the membrane-embedded domain of an inward rectifier K+ channel protein Kir5.1. 

Figure1. Removable Arg-tagged backbone modification for chemical synthesis of membrane proteins

Reference:

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1.Zheng, J. S. et al. Expedient total synthesis of small to medium-sized membrane proteins via Fmoc chemistry. Journal of the American Chemical Society136, 3695-3704, doi:10.1021/ja500222u (2014).

2. Zheng, J. S. et al. Robust Chemical Synthesis of Membrane Proteins through a General Method of Removable Backbone Modification. Journal of the American Chemical Society138, 3553-3561, doi:10.1021/jacs.6b00515 (2016).

3. Li, J. B., Tang, S., Zheng, J. S., Tian, C. L. & Liu, L. Removable Backbone Modification Method for the Chemical Synthesis of Membrane Proteins. Accounts of chemical research50, 1143-1153, doi:10.1021/acs.accounts.7b00001 (2017).