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Issue 5, 2017
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Chemical synthesis of a homoserine-mutant of the antibacterial, head-to-tail cyclized protein AS-48 by α-ketoacid–hydroxylamine (KAHA) ligation

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Abstract

An antibacterial cyclic AS-48 protein was chemically synthesized by α-ketoacid–hydroxylamine (KAHA) ligation. Initial challenges associated with the exceptionally hydrophobic segments arising from the amphiphilic nature of the protein were resolved by the development of bespoke reaction conditions for hydrophobic segments, using hexafluoroisopropanol (HFIP) as a co-solvent. The synthetic protein displays similar biological activity and properties to those of the native protein. To support the current understanding of its antibacterial mode of action, we demonstrate the ability of AS-48 to be incorporated into synthetic multilamellar vesicles (MLVs).

Graphical abstract: Chemical synthesis of a homoserine-mutant of the antibacterial, head-to-tail cyclized protein AS-48 by α-ketoacid–hydroxylamine (KAHA) ligation

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Publication details

The article was received on 19 Feb 2017, accepted on 23 Mar 2017 and first published on 24 Mar 2017


Article type: Edge Article
DOI: 10.1039/C7SC00789B
Citation: Chem. Sci., 2017,8, 4051-4055
  • Open access: Creative Commons BY-NC license
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    Chemical synthesis of a homoserine-mutant of the antibacterial, head-to-tail cyclized protein AS-48 by α-ketoacid–hydroxylamine (KAHA) ligation

    F. Rohrbacher, A. Zwicky and J. W. Bode, Chem. Sci., 2017, 8, 4051
    DOI: 10.1039/C7SC00789B

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