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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
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Structural basis for antimicrobial activity of lasiocepsin
Lenka Monincová1, Milos Buděšínský, Sabina Čujová
1Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 16610 Prague 6 (Czech Republic).
Chembiochem : a European Journal of Chemical Biology
|December 17, 2013
Summary
Lasiocepsin, a peptide from wild bee venom, exhibits potent antibacterial and antifungal properties. It effectively targets bacterial membranes, particularly those rich in cardiolipin.
Area of Science:
- Biochemistry
- Microbiology
- Peptide Science
Background:
- Antimicrobial peptides (AMPs) are crucial in innate immunity.
- Wild bee venom contains diverse bioactive compounds, including peptides.
- Lasiocepsin is a novel peptide isolated from Lasioglossum laticeps venom.
Purpose of the Study:
- To characterize the structure and function of lasiocepsin.
- To investigate its antimicrobial activity and mechanism of action.
- To explore its potential as a therapeutic agent.
Main Methods:
- Peptide isolation and purification from bee venom.
- Structural analysis using spectroscopic techniques.
- Antimicrobial assays against various bacterial and fungal strains.
- Lipid-binding studies and membrane interaction experiments.
Main Results:
- Lasiocepsin is a 27-residue peptide with a distinct amphipathic structure featuring two alpha-helices.
- It displays significant antibacterial and antifungal activity.
- The peptide shows a strong preference for anionic phospholipids, especially cardiolipin.
- Membrane permeabilization is initiated at the N-terminus and is dependent on cardiolipin concentration.
Conclusions:
- Lasiocepsin is a potent antimicrobial peptide with a unique structure and mechanism of action.
- Its cardiolipin-binding preference suggests targeted activity against bacteria.
- Further research may lead to the development of lasiocepsin-based antimicrobials.
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