Antimicrobial activity of human hepcidin 20 and 25 against clinically relevant bacterial strains Effect of copper and acidic pH

作者：Maisetta Giuseppantonio; Petruzzelli Raffaele; Brancatisano Franca Lisa; Esin Semih; Vitali Alberto; Campa Mario; Batoni Giovanna^*

来源：Peptides, 2010, 31(11): 1995-2002.

DOI：10.1016/j.peptides.2010.08.007

• Antimicrobial peptides
• Hepcidin 20
• Hepcidin 25
• Copper
• pH
• Multi drug resistance

Hepcidin 25 (hep-25) is a peptide primarily produced by human liver with a central role in iron homeostasis Its isoform hepcidin 20 (hep-20) has an unknown function and lacks the first five aminoacids of the amino-terminal portion This sequence is crucial for Iron regulation by hep-25 and contains a molecular motif able to bind metals Aim of this study was to evaluate the antibacterial properties of both peptides in vitro against a wide range of bacterial clinical isolates and in different experimental conditions Although both peptides were found to be bactericidal against a variety of clinical isolates with different antibiotic resistance profiles hep-20 was active at lower concentrations than hep-25 in most of the cases Killing kinetics carried on in sodium-phosphate buffer at pH 7 4 demonstrated that bactericidal activity occurred not earlier than 30-90 min of incubation Bactericidal activity of hep-25 was slightly enhanced in the presence of copper while the same metal did not affect the activity of hep-20 Interestingly bactericidal activity of both hepcidins was highly enhanced at acidic pH Acidic pH (pH 5 0 and 6 6) not only reduced the microbicidal concentrations of hepcidins but also shortened the killing times of both peptides as compared to pH 7 4 Combining hep-20 and hep-25 at pH 5 0 a bactericidal effect could be obtained at very low concentrations of both peptides

• 出版日期2010-11