Publication Database

Fine‐tuning the antimicrobial activity of β‐hairpin peptides with fluorinated amino acids (2023)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Chowdhary, Suvrat

Pelzer, Tim

Saathoff, Mareike (WE 7)

Quaas, Elisa

Pendl, Johanna

Fulde, Marcus (WE 7)

Koksch, Beate

Quelle

Journal of peptide science : an official publication of the European Peptide Society

Bandzählung: 115

Heftzählung: 3

Seiten: e24306

ISSN: 1075-2617

Sprache

Englisch

Verweise

URL (Volltext): https://onlinelibrary.wiley.com/doi/10.1002/pep2.24306

DOI: 10.1002/pep2.24306

Kontakt

Institut für Mikrobiologie und Tierseuchen

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51843 / 66949
mikrobiologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

Antimicrobial peptides (AMPs) possess bactericidal activity against a variety of pathogensdepending on an overall balance of positivelycharged and hydrophobic residues. Selec-tive fluorination of peptides serves to fine-tune the intrinsic hydrophobicity and thatcould improve AMP bioactivity without affecting the sequence length. Only a few studieshave focused on the impact of this unique element on antimicrobial potency and cameto somewhat contractionary results. Moreover, the influence of fluorinated amino acidson peptide proteolysis is yet not fully understood. In this work, we tackle the linkbetween side chain fluorination and both antimicrobial activity and proteolytic stabilityfor two series of amphiphilicβ-hairpin peptides. In particular, a synergy between antimi-crobial activity and peptide hydrophobicitywas determined. All peptides were found tobe barely hemolytic and non-toxic. Most surprisingly, the fluorinated peptides were sus-ceptible to enzymatic degradation. Hence, the distinctive properties of these polyfluori-nated AMPs will serve for the future design of peptide-based drugs.