Truncated and constrained helical analogs of antimicrobial esculentin-2EM

Thanh Kim Pham, Do Hee Kim, Bong Jin Lee, Young Woo Kim

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Esculentin-2EM is a 37-residue, cationic, amphipathic, α-helical antimicrobial peptide isolated from a Korean frog, Glandirama emeljanovi. Many studies revealed that truncation of this peptide results in substantial decreases in its antimicrobial activity. Lee and his colleagues have recently reported that a 23-residue esculentin-2EM analog containing a tryptophanyl substitution at position 16 showed a significant recovery of the antimicrobial activity of the parent peptide. Here we report a new series of 15-residue esculentin-2EM analogs which are constrained into an α-helical conformation via an oct-4-enyl cross-link. The resulting 'stapled' derivatives displayed remarkable increases not only in antimicrobial activity but also in helical content and protease resistance compared to Lee's original 23-residue esculentin-2EM analog. The preliminary data obtained in this work strongly supports the potential of our strategy for the development of a new class of peptide antibiotics.

Original languageEnglish
Pages (from-to)6717-6720
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume23
Issue number24
DOIs
StatePublished - 15 Dec 2013

Keywords

  • Antimicrobial peptides
  • Esculentin-2EM
  • Proteolytic resistance
  • Stapled peptides
  • α-Helix

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