Antifungal Activities of Peptides Derived from Domain 5 of High-Molecular-Weight Kininogen
Degradation of HMWK generates antifungal peptides. (a) Intact HMWK and cleavage products from different incubations (indicated below, human leukocyte elastase, HLE, and polymorphonuclear neutrophils, PMN), were analyzed by SDS-PAGE (16.5% Tris-Tricine gel). (b) Antifungal activity of HMWK cleavage products is shown as clear zones corresponding to inhibition of fungal growth in RDA. Cleavage of HMWK was performed for 30 and 60 minutes at 37°C. (1) control, buffer (10 mM Tris, pH 7.4). (2) reference, LL-37 (6 μL at 100 μM). (3) control, HMWK. (4) control, human leukocyte elastase (HLE). (5) and (6) HMWK incubated with HLE for 30 and 60 minutes, respectively. (7) control, polymorphonuclear neutrophils (PMN). (8) and (9) HMWK incubated with PMN for 30 and 60 minutes, respectively. Data represents the results from a single representative experiment out of three. (c) HMWK was subjected to Cathepsin G, producing cleavage products recognized by polyclonal antibodies against HKH20 by Western blot analysis. In the panels, molecular mass markers are indicated on the left.
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