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Antimicrobial Agents and Chemotherapy, August 2005, p. 3387-3395, Vol. 49, No. 8
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.8.3387-3395.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Human Lactoferricin Is Partially Folded in Aqueous Solution and Is Better Stabilized in a Membrane Mimetic Solvent

Howard N. Hunter,1 A. Ross Demcoe,1 Håvard Jenssen,2 Tore J. Gutteberg,2 and Hans J. Vogel1*

Department of Biological Sciences, University of Calgary, 2500 University Drive, N.W., Calgary, Alberta, Canada T2N 1N4,1 Department of Medical Microbiology, University Hospital of North Norway, N-9038 Tromsø, Norway2

Received 13 February 2005/ Returned for modification 18 March 2005/ Accepted 15 April 2005

Lactoferricins are highly basic bioactive peptides that are released in the stomach through proteolytic cleavage of various lactoferrin proteins. Here we have determined the solution structure of human lactoferricin (LfcinH) by conventional two-dimensional nuclear magnetic resonance methods in both aqueous solution and a membrane mimetic solvent. Unlike the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat distorted antiparallel ß sheet, the longer LfcinH peptide shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent ß-sheet character in either the N- or C-terminal regions of the peptide. The helical characteristic of the LfcinH peptide resembles the conformation that this region adopts in the crystal structure of the intact protein. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. Numerous hydrophobic interactions create the basis for the better-defined overall structure observed in the membrane mimetic solvent. The 49-residue LfcinH peptide isolated for these studies was found to be slightly longer than previously reported peptide preparations and was found to have an intact peptide bond between residues Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB represent a novel difference in the physical properties of these two peptides, which contributes to their unique physiological activities.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Calgary, 2500 University N.W., Calgary, Alberta, Canada T2N 1N4. Phone: (403) 220-6006. Fax: (403) 289-9311. E-mail: vogel{at}ucalgary.ca.

Antimicrobial Agents and Chemotherapy, August 2005, p. 3387-3395, Vol. 49, No. 8
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.8.3387-3395.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jenssen, H., Hamill, P., Hancock, R. E. W. (2006). Peptide Antimicrobial Agents. Clin. Microbiol. Rev. 19: 491-511 [Abstract] [Full Text]  


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