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Updated: Feb 11, 2026

Influenza A Virus Studies in a Mouse Model of Infection
Published on: September 7, 2017
Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel
A C Baumruck1, D Tietze2, L K Steinacker1
1Darmstadt University of Technology , Clemens-Schöpf Institute of Organic Chemistry and Biochemistry , Alarich-Weiss Str. 4 , 64287 Darmstadt , Germany .
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).
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