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BioMed Research International
Volume 2017 (2017), Article ID 5130495, 10 pages
Research Article

Structure and Function of Trypsin-Loaded Fibrinolytic Liposomes

1Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
2IMEC, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary

Correspondence should be addressed to Krasimir Kolev

Received 3 February 2017; Revised 12 April 2017; Accepted 4 May 2017; Published 3 July 2017

Academic Editor: Zsuzsa Bagoly

Copyright © 2017 Anna Tanka-Salamon et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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 () and characterize their structure and fibrinolytic efficiency. Hydrogenated soybean phosphatidylcholine-based 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 hydrophilic/hydrophobic interface (FT-IR). The thermosensitivity of was evidenced by enhanced fibrinolysis at 45°C: time to reduce the maximal turbidity to 20% decreased by 8.6% compared to 37°C and fibrin degradation product concentration in the permeation lysis assay was 2-fold to 5-fold higher than that at 24°C. exerted its fibrinolytic action on fibrin clots under both static and dynamic conditions, whereas plasma clot dissolution was observed only in the permeation-driven assay. The improved fibrinolytic efficiency of under dynamic conditions suggests that they may serve as a novel therapeutic candidate for dissolution of intravascular thrombi, which are typically exposed to permeation forces.