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Antimicrobial Agents and Chemotherapy, March 2003, p. 965-971, Vol. 47, No. 3
0066-4804/03/$08.00+0 DOI: 10.1128/AAC.47.3.965-971.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Helsinki Biophysics & Biomembrane Group, Institute of Biomedicine, FIN-00014 University of Helsinki, Finland
Received 3 September 2002/ Returned for modification 15 October 2002/ Accepted 23 December 2002
The antimicrobial peptides magainin 2, indolicidin, and temporins B and L were found to modulate the hydrolytic activity of secretory phospholipase A2 (sPLA2) from bee venom and in human lacrimal fluid. More specifically, hydrolysis of phosphatidylcholine (PC) liposomes by bee venom sPLA2 at 10 µM Ca2+ was attenuated by these peptides while augmented product formation was observed in the presence of 5 mM Ca2+. The activity of sPLA2 towards anionic liposomes was significantly enhanced by the antimicrobial peptides at low [Ca2+] and was further enhanced in the presence of 5 mM Ca2+. Similarly, with 5 mM Ca2+ the hydrolysis of anionic liposomes was enhanced significantly by human lacrimal fluid sPLA2, while that of PC liposomes was attenuated. These results indicate that concerted action of antimicrobial peptides and sPLA2 could improve the efficiency of the innate response to infections. Interestingly, inclusion of a cationic gemini surfactant in the vesicles showed an essentially similar pattern on sPLA2 activity, suggesting that the modulation of the enzyme activity by the antimicrobial peptides may involve also charge properties of the substrate surface.
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