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Antimicrobial Agents and Chemotherapy, June 2004, p. 2097-2100, Vol. 48, No. 6
0066-4804/04/$08.00+0 DOI: 10.1128/AAC.48.6.2097-2100.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden,1 Department of Pediatrics, University of Göttingen, D-37075 Göttingen, Germany2
Received 3 September 2003/ Returned for modification 14 October 2003/ Accepted 6 February 2004
The antibacterial activities of the cathelicidin peptides LL-37 and an 18-residue C-terminal fragment of prophenin, corresponding to positions 62 to 79 of native prophenin (PF-18), were analyzed in the presence of a modified surfactant preparation isolated from minced porcine lungs. At low micromolar concentrations, both LL-37 and PF-18 showed significant activities against different serotypes of group B streptococci, with LL-37 being more active on a molar basis. The surfactant preparation at a concentration of 10 mg/ml partly blocked the antibacterial activity of 9 µM LL-37 and completely blocked the antibacterial activity of 9 µM PF-18. However, 10 mg of the surfactant preparation per ml had only minor inhibitory effects on LL-37 and PF-18 at 90 µM. Addition of up to 900 µM PF-18 did not affect the surface properties of the surfactant preparation. These data suggest that surfactant preparations containing antimicrobial peptides could be useful for the local treatment of pulmonary infections.
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