ArticleRSC chemical biology2021
A mixed chirality α-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography.
Article in RSC chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Purification, Characterization, and In Vitro Safety Assessment of the Antimicrobial Peptide SAM-KB40 from Bacillus licheniformis SAM-D318.Applied biochemistry and biotechnology · 2026Article
- Microchiral pinwheel arrays based on achiral molecules.Nature communications · 2026Article
- Antimicrobial Peptide-Peptoid Macrocycles from the Polymyxin B2 Chemical Space.Angewandte Chemie (International ed. in English) · 2025Article
- Stereorandomized Oncocins with Preserved Ribosome Binding and Antibacterial Activity.Journal of medicinal chemistry · 2024Article
- The Mystery of Homochirality on Earth.Life (Basel, Switzerland) · 2024Review
- Antimicrobial Peptide-Peptoid Hybrids with and without Membrane Disruption.ACS infectious diseases · 2023Article
- To Fold or Not to Fold: Diastereomeric Optimization of an α-Helical Antimicrobial Peptide.Journal of medicinal chemistry · 2023Article
- Dipropylamine for 9-Fluorenylmethyloxycarbonyl (Fmoc) Deprotection with Reduced Aspartimide Formation in Solid-Phase Peptide Synthesis.ACS omega · 2023Article
- An intrinsically disordered antimicrobial peptide dendrimer from stereorandomized virtual screening.Cell reports. Physical science · 2022Article
- Machine Learning Guided Discovery of Non-Hemolytic Membrane Disruptive Anticancer Peptides.ChemMedChem · 2022Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peptide α-helix is right-handed when containing amino acids with l-chirality, and left-handed with d-chirality, however mixed chirality peptides generally do not form α-helices unless a helix inducer such as the non-natural residue amino-isobutyric acid is used. Herein we report the first X-ray crystal structures of mixed chirality α-helices in short peptides comprising only natural residues as the example of a stapled bicyclic and a linear membrane disruptive amphiphilic antimicrobial peptide (AMP) containing seven l- and four d-residues, as complexes of fucosylated analogs with the bacterial lectin LecB. The mixed chirality α-helices are superimposable onto the homochiral α-helices and form under similar conditions as shown by CD spectra and MD simulations but non-hemolytic and resistant to proteolysis. The observation of a mixed chirality α-helix with only natural residues in the protein environment of LecB suggests a vast unexplored territory of α-helical mixed chirality sequences and their possible use for optimizing bioactive α-helical peptides.
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