ArticleNature protocols2017
Chemical synthesis of membrane proteins by the removable backbone modification method.
Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Chemical Synthesis of Human Proteoforms and Application in Biomedicine.ACS central science · 2024Review
- Enhanced native chemical ligation by peptide conjugation in trifluoroacetic acid.Science advances · 2024Article
- Article
- A glutamic acid-based traceless linker to address challenging chemical protein syntheses.Organic & biomolecular chemistry · 2021Article
- Effect of Methionine Sulfoxide on the Synthesis and Purification of Aggregation-Prone Peptides.Chembiochem : a European journal of chemical biology · 2021Article
- Native Chemical Ligation of Highly Hydrophobic Peptides in Ionic Liquid-Containing Media.The Journal of organic chemistry · 2021Article
- A straightforward methodology to overcome solubility challenges for N-terminal cysteinyl peptide segments used in native chemical ligation.Chemical science · 2021Article
- Challenges and Perspectives in Chemical Synthesis of Highly Hydrophobic Peptides.Frontiers in bioengineering and biotechnology · 2020Review
- Diselenide-selenoester ligation for chemical protein synthesis.Nature protocols · 2019Article
- Channel activity of mirror-image M2 proton channel of influenza A virus is blocked by achiral or chiral inhibitors.Protein & cell · 2019Article
- Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel.Chemical science · 2018Article
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Authors and funding
8 authors.
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Abstract
Chemical synthesis can produce membrane proteins bearing specifically designed modifications (e.g., phosphorylation, isotope labeling) that are difficult to obtain through recombinant protein expression approaches. The resulting homogeneously modified synthetic membrane proteins are valuable tools for many advanced biochemical and biophysical studies. This protocol describes the chemical synthesis of membrane proteins by condensation of transmembrane peptide segments through native chemical ligation. To avoid common problems encountered due to the poor solubility of transmembrane peptides in almost any solvent, we describe an effective procedure for the chemical synthesis of membrane proteins through the removable-backbone modification (RBM) strategy. Two key steps of this protocol are: (i) installation of solubilizing Arg4-tagged RBM groups into the transmembrane peptides at any primary amino acid through Fmoc (9-fluorenylmethyloxycarbonyl) solid-phase peptide synthesis and (ii) native ligation of the full-length sequence, followed by removal of the RBM tags by TFA (trifluoroacetic acid) cocktails to afford the native protein. The installation of RBM groups is achieved by using 4-methoxy-5-nitrosalicyladehyde by reduction amination to incorporate an activated O-to-N acyl transfer auxiliary. The Arg4-tag-modified membrane-spanning peptide segments behave like water-soluble peptides to facilitate their purification, ligation and mass characterization.
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