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Shortened cecropin A‐melittin hybrids Significant size reduction retains potent antibiotic activity
Author(s) -
Andreu David,
Ubach Josep,
Boman Anita,
Wåhlin Birgitta,
Wade David,
Merrifield R.B.,
Boman Hans G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80377-s
Subject(s) - melittin , cecropin , peptide , antibiotics , residue (chemistry) , antibacterial activity , chemistry , membrane , defensin , biochemistry , bacteria , biology , antimicrobial peptides , genetics
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.