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Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation
Bruno Casciaro1, Daniel Ben Hur2, Daniela Roversi3
1Laboratory Affiliated to Pasteur Italia-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Sapienza University of Rome, Rome, Italy.
Summary
Novel antimicrobial peptides (AMPs) with enhanced stability and reduced toxicity were developed. Esc(1-21)ε20 analogs show potent activity against Gram-negative bacteria, offering a promising alternative to conventional antibiotics.
Area of Science:
- Biochemistry
- Microbiology
- Pharmacology
Background:
- Antimicrobial peptides (AMPs) disrupt bacterial membranes but face challenges like cytotoxicity and low biostability.
- Esc(1-21), a frog-skin derived AMP, shows potent activity against Gram-negative bacteria.
Purpose of the Study:
- To design and synthesize novel Esc(1-21) analogs with improved properties.
- To evaluate these analogs for antimicrobial efficacy, stability, and safety.
Main Methods:
- Synthesized five Esc(1-21) analogs incorporating isopeptide bonds.
- Assessed chemical/structural properties, proteolytic resistance, antimicrobial/antibiofilm activity, cytotoxicity, and membrane perturbation.
Main Results:
- Esc(1-21)ε20 demonstrated comparable antimicrobial and antibiofilm activity to the parent peptide.
- Esc(1-21)ε20 exhibited reduced cytotoxicity and enhanced resistance to enzymatic degradation.
- The analogs' ability to perturb bacterial membranes was evaluated.
Conclusions:
- Esc(1-21)ε20 is a promising lead candidate for novel antibiotic development.
- Isopeptide bond incorporation enhances AMP biostability and safety profiles.
- This strategy offers a viable approach to overcome AMP clinical limitations.
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