A mixed chirality α-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography-Reference-Cited by-同舟云学术

A mixed chirality α-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography

Published:2021 Issue:6 Volume:2 Page:1608-1617
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Baeriswyl Stéphane¹^ORCID,Personne Hippolyte¹^ORCID,Di Bonaventura Ivan¹^ORCID,Köhler Thilo²^ORCID,van Delden Christian²^ORCID,Stocker Achim¹^ORCID,Javor Sacha¹^ORCID,Reymond Jean-Louis¹^ORCID

Affiliation:

1. Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland

2. Department of Microbiology and Molecular Medicine, University of Geneva, Service of Infectious Diseases, University Hospital of Geneva, Geneva, Switzerland

Abstract

We report the first X-ray crystal structures of mixed chirality α-helices comprising only natural residues as the example of bicyclic and linear membrane disruptive amphiphilic antimicrobial peptides containing seven l- and four d-residues.

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

H2020 European Research Council

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CB/D1CB00124H

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