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Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity

Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity We have earlier reported two 26‐residue antibacterial peptides made up from different segments ol'cecropin A (CA) and melittin (M). We now report a substantial reduction in size at the C‐terminal section of the highly active hybrid CA(1–8)M(1–18), leading to a series of 20‐, 18‐ and 15‐residue analogs with antibiotic properties similar to the larger molecule. In particular, the 15‐residue hybrids CA(1–7)M(2–9), CA(1–7)M(4–11) and CA(1–7)M(5–12) are the shortest cecropin‐based peptide antibiotics described so far, with antibacterial activity and spectra similar or better than cecropin A and a 60% reduction in size. Their reduced size and highly α‐helical structure require an alternative mechanism for their interaction with bacterial membranes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Febs Letters Wiley

Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity

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References (24)

Publisher
Wiley
Copyright
© 2015 Federation of European Biochemical Societies
eISSN
1873-3468
DOI
10.1016/0014-5793(92)80377-S
Publisher site
See Article on Publisher Site

Abstract

We have earlier reported two 26‐residue antibacterial peptides made up from different segments ol'cecropin A (CA) and melittin (M). We now report a substantial reduction in size at the C‐terminal section of the highly active hybrid CA(1–8)M(1–18), leading to a series of 20‐, 18‐ and 15‐residue analogs with antibiotic properties similar to the larger molecule. In particular, the 15‐residue hybrids CA(1–7)M(2–9), CA(1–7)M(4–11) and CA(1–7)M(5–12) are the shortest cecropin‐based peptide antibiotics described so far, with antibacterial activity and spectra similar or better than cecropin A and a 60% reduction in size. Their reduced size and highly α‐helical structure require an alternative mechanism for their interaction with bacterial membranes.

Journal

Febs Letters – Wiley

Published: Jan 20, 1992

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