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Issue 8, 2018
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Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel

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Abstract

In the present study we have developed and optimized a robust strategy for the synthesis of highly hydrophobic peptides, especially membrane proteins, exemplarily using the influenza B M2 proton channel (BM2(1–51)). This strategy is based on the native chemical ligation of two fragments, where the thioester fragment is formed from an oxo-ester peptide, which is synthesized using Fmoc-SPPS, and features an in situ cleavable solubilizing tag (ADO, ADO2 or ADO-Lys5). The nearly quantitative production of the ligation product was followed by an optimized work up protocol, resulting in almost quantitative desulfurization and Acm-group cleavage. Circular dichroism analysis in a POPC lipid membrane revealed that the synthetic BM2(1–51) construct adopts a helical structure similar to that of the previously characterized BM2(1–33).

Graphical abstract: Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel

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Publication details

The article was received on 01 Jan 2018, accepted on 21 Jan 2018 and first published on 22 Jan 2018


Article type: Edge Article
DOI: 10.1039/C8SC00004B
Citation: Chem. Sci., 2018,9, 2365-2375
  • Open access: Creative Commons BY license
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    Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel

    A. C. Baumruck, D. Tietze, L. K. Steinacker and A. A. Tietze, Chem. Sci., 2018, 9, 2365
    DOI: 10.1039/C8SC00004B

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