DNase I functional microgels for neutrophil extracellular trap disruption
Aisa Hosseinnejad, Nadine Ludwig, Ann-Katrin Wienkamp, Rahul Rimal, Christian Bleilevens, Rolf Rossaint, Jan Rossaint, Smriti Singh
Abstract
value representing the enzymatic activity of the conjugated DNase I was calculated to be 0.063 μM demonstrating a high enzyme-substrate affinity. The DNase I MGs were protein repellant and were able to digest NETs more efficiently compared to free DNase in a biological media, remarkably even after long-term exposure to the stimulated neutrophils continuously releasing NETs. Overall, the conjugation of DNase I to a non-fouling microgel provides a novel biohybrid platform that can be exploited as non-thrombogenic active microgel-based coatings for blood-contacting surfaces to reduce the NET-mediated inflammation and microthrombi formation.