Structure and Function of Trypsin-Loaded Fibrinolytic Liposomes.

ABSTRACT: Protease encapsulation and its targeted release in thrombi may contribute to the reduction of haemorrhagic complications of thrombolysis. We aimed to prepare sterically stabilized trypsin-loaded liposomes (SSL_T) and characterize their structure and fibrinolytic efficiency. Hydrogenated soybean phosphatidylcholine-based SSL_T were prepared and their structure was studied by transmission electron microscopy combined with freeze fracture (FF-TEM), Fourier transform infrared spectroscopy (FT-IR), and small-angle X-ray scattering (SAXS). Fibrinolytic activity was examined at 45, 37, or 24°C on fibrin or plasma clots with turbidimetric and permeation-driven lysis assays. Trypsin was shown to be attached to the inner surface of vesicles (SAXS and FF-TEM) close to the lipid hy

SUBMITTER: Tanka-Salamon A 

PROVIDER: S-EPMC5512056 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature