Structural basis for antimicrobial activity of lasiocepsin

Chembiochem. 2014 Jan 24;15(2):301-8. doi: 10.1002/cbic.201300509. Epub 2013 Dec 12.


Lasiocepsin is a unique 27-residue antimicrobial peptide, isolated from Lasioglossum laticeps (wild bee) venom, with substantial antibacterial and antifungal activity. It adopts a well-defined structure consisting of two α-helices linked by a structured loop. Its basic residues form two distinct positively charged regions on the surface whereas aliphatic side chains contribute to solvent-accessible hydrophobic areas, thus emphasising the amphipathic character of the molecule. Lasiocepsin structurally belongs to the ShK family and shows a strong preference for anionic phospholipids; this is further augmented by increasing concentrations of cardiolipin, such as those found at the poles of bacterial cells. The membrane-permeabilising activity of the peptide is not limited to outer membranes of Gram-negative bacteria. The peptide interacts with phospholipids initially through its N terminus, and its degree of penetration is strongly dependent on the presence of cardiolipin.

Keywords: Lasioglossum laticeps; NMR spectroscopy; ShK family; antimicrobial peptides; membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / metabolism
  • Anti-Infective Agents / pharmacology*
  • Bee Venoms / chemistry*
  • Bee Venoms / metabolism
  • Bee Venoms / pharmacology*
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Escherichia coli / cytology
  • Escherichia coli / drug effects
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / metabolism
  • Peptides, Cyclic / pharmacology*
  • Permeability
  • Protein Conformation
  • Protein Transport


  • Anti-Infective Agents
  • Bee Venoms
  • Peptides, Cyclic
  • lasiocepsin