The lung pathogenesis of cystic fibrosis (CF) involves inflammation, airway obstruction and an increased incidence of pulmonary infections. Increased levels of proinflammatory cytokines and chemokines such as interleukin-8 (IL-8) play a pivotal role in sustaining the cycle of inflammation in the CF lung. Glycosaminoglycans (GAGs) possess the ability to bind IL-8 providing protection from proteolytic degradation and maintaining it in an active state leading to sustained neutrophil chemotaxis. It has been shown that hypertonic saline (HTS) disrupts GAG:IL-8 complexes, thus rendering IL-8 susceptible to proteolysis thereby reducing neutrophil chemotaxis. The recombinant IL-8 decoy (PA401) binds glycans with higher affinity (x 40) than native IL-8. In this study, we compared the ability of PA401 and HTS to disrupt IL-8:GAG complexes in CF BALF.