Structure and Function of Trypsin-Loaded Fibrinolytic Liposomes.
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 (SSLT) and characterize their structure and fibrinolytic efficiency. Hydrogenated soybean phosp...
| Publicado en: | BioMed Research International Vol. 2017; pp. 1 - 11 |
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| Autores principales: | , , , , , |
| Formato: | research tables/charts Journal Article |
| Publicado: |
Wiley-Blackwell
7/3/2017
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=123912610&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 123912610 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 7/3/2017 vid: 2017 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 123912610 123912610 123912610 10.1155/2017/5130495 123912610 ppf: 1 ppct: 10 formats: fmt: @attributes: type: P tig: atl: Structure and Function of Trypsin-Loaded Fibrinolytic Liposomes. aug: au: Tanka-Salamon, Anna Bóta, Attila Wacha, András Mihály, Judith Lovas, Miklós Kolev, Krasimir affil: Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary sug: subj: Trypsin Fibrinolytic Agents Phospholipids Thrombolytic Therapy Adverse Effects Human Soybeans Spectrophotometry, Infrared Microscopy, Electron Fibrin Physiology Funding Source Mass Spectrometry ab: 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 (SSLT) and characterize their structure and fibrinolytic efficiency. Hydrogenated soybean phosphatidylcholine-based SSLT 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 SSLT 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. SSLT 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 SSLT 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. pubtype: Academic Journal doctype: research tables/charts Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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