The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles

FEBS Lett. 1999 Mar 12;446(2-3):213-7. doi: 10.1016/s0014-5793(99)00214-8.

Abstract

Lactoferricin B (LfcinB) is a 25-residue antimicrobial peptide released from bovine lactoferrin upon pepsin digestion. The antimicrobial center of LfcinB consists of six residues (RRWQWR-NH2), and it possesses similar bactericidal activity to LfcinB. The structure of the six-residue peptide bound to sodium dodecyl sulfate (SDS) micelles has been determined by NMR spectroscopy and molecular dynamics refinement. The peptide adopts a well defined amphipathic structure when bound to SDS micelles with the Trp sidechains separated from the Arg residues. Additional evidence demonstrates that the peptide is oriented in the micelle such that the Trp residues are more deeply buried in the micelle than the Arg and Gln residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / metabolism
  • Cattle
  • Circular Dichroism
  • Lactoferrin / analogs & derivatives*
  • Lactoferrin / chemistry
  • Lactoferrin / metabolism
  • Micelles*
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides*
  • Protein Conformation*
  • Sodium Dodecyl Sulfate* / chemistry
  • Sodium Dodecyl Sulfate* / metabolism

Substances

  • Anti-Bacterial Agents
  • Micelles
  • Peptides
  • lactoferricin B
  • Sodium Dodecyl Sulfate
  • Lactoferrin