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How are 1,2,3-triazoles accommodated in helical secondary structures?

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Abstract

1,4-Disubstituted-1,2,3-triazole (Tz) is widely used in peptides as a trans-amide bond mimic, despite having hazardous effects on the native peptide activity. The impact of amide bond substitution by Tz on peptide secondary structures is scarcely documented. We performed a Tz scan, by systematically replacing peptide bonds following the Aib residues with Tz on two model peptaibols: alamethicin F50/5 and bergofungin D, which adopt stable α- and 310 helices, respectively. We observed that the Tz insertion, whatever its position in the peptide sequences, abolished their antimicrobial activity. The structural consequences of this insertion were further investigated using CD, NMR and X-ray diffraction. Importantly, five crystal structures that were incorporated with Tz were solved, showing various degrees of alteration of the helical structures, from minor structural perturbation of the helix to partial disorder. Together, these results showed that Tz insertions impair helical secondary structures.

Graphical abstract: How are 1,2,3-triazoles accommodated in helical secondary structures?

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Publication details

The article was received on 20 Mar 2018, accepted on 12 Apr 2018 and first published on 12 Apr 2018


Article type: Paper
DOI: 10.1039/C8OB00686E
Citation: Org. Biomol. Chem., 2018, Advance Article
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    How are 1,2,3-triazoles accommodated in helical secondary structures?

    K. Ben Haj Salah, S. Das, N. Ruiz, V. Andreu, J. Martinez, E. Wenger, M. Amblard, C. Didierjean, B. Legrand and N. Inguimbert, Org. Biomol. Chem., 2018, Advance Article , DOI: 10.1039/C8OB00686E

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