Johansson, Jan
- Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
Sammanfattning
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 muM LL-37 and completely blocked the antibacterial activity of 9 muM PF-18. However, 10 mg of the surfactant preparation per ml had only minor inhibitory effects on LL-37 and PF-18 at 90 muM. Addition of up to 900 muM 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.
Publicerad i
Antimicrobial Agents and Chemotherapy
2004, volym: 48, nummer: 6, sidor: 2097-2100
Utgivare: AMER SOC MICROBIOLOGY
SLU författare
UKÄ forskningsämne
Farmaceutisk vetenskaper
Publikationens identifierare
- DOI: https://doi.org/10.1128/AAC.48.6.2097-2100.2004
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/3298