Protein-liposome conjugates with defined size distributions

Loughrey, Helen; Wong, Kenneth; Choi, Lewis S. L.; Cullis, Pieter R.; Bally, Marcel B.

doi:10.1016/0005-2736(90)90267-r

Cited by 32 publications

(16 citation statements)

References 19 publications

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“…These results indicate that the aggregation of the HbV is induced by some specific interaction with plasma components. It is reported that the phospholipid vesicles, especially the negatively charged vesicles, adsorb the plasma proteins such as albumin and lipoproteins (Hernandez‐Caselles et al, 1993; Loughrey et al, 1990), which leads to a decrease in the dispersibility of the vesicles. We confirmed that the adsorbed proteins on the vesicular surface were major plasma proteins such as albumin and globulin (Ohgushi et al; 1994).…”

Section: Resultsmentioning

confidence: 99%

Physical Properties of Hemoglobin Vesicles as Red Cell Substitutes

et al. 1996

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Hemoglobin vesicles (HbV) as red cell substitutes were prepared from a purified carbonylhemoglobin (HbCO) solution and a lipid mixture composed of phospholipids, cholesterol, and alpha-tocopherol. The diameter was controlled to 251 +/- 87 nm using an extrusion method; the vesicles penetrated through the membrane filters with regulated pore sizes. After the ligand exchanging reaction (HbCO-->HbO2), the oxygen affinity (P50) of HbV was 32 Torr, which was controlled with the coencapsulation of pyridoxal 5'-phosphate. The rate of metHb formation in HbV was nonenzymatically reduced with the coencapsulation of DL-homocysteine. The Hb concentration of the HbV suspension, which was dispersed in a phosphate buffered saline solution (pH 7.4), was controlled at 10 g/dL. At this concentration, the total lipid concentration was 6.2 g/dL and the viscosity, 2.6 cP (230 s-1), was lower than that of the blood (4.4 cP). The HbV suspension showed a typical non-Newtonian flow for a particle dispersion and agreed well with the Casson model. The viscosity at shear rates lower than 23 s-1 showed a maximum with increasing the mixing ratio of human blood, plasma, or albumin, while no maximum was observed for the mixture with washed red blood cells. The aggregates of HbV are formed by interaction with plasma proteins, including albumin, while the aggregates reversibly dissociate at higher shear rate.

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Section: Resultsmentioning

confidence: 99%

Physical Properties of Hemoglobin Vesicles as Red Cell Substitutes

et al. 1996

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“…Another method is post-functionalization which attaches the proteins to the liposome surface by preparing the liposome first with anchor lipid followed by the conjugation of protein and anchor lipid. However, problems always arise from the cross-linking reactions and resulting aggregation of liposomes and lower coupling yields (15). Moreover, the liposome size may alter after the conjugation, which affects the clearance behavior in vivo (16).…”

Section: Resultsmentioning

confidence: 99%

Recombinant and chemo-/bio-orthogonal synthesis of liposomal thrombomodulin and its antithrombotic activity

Wang

Jiang

Liu

et al. 2017

Journal of Bioscience and Bioengineering

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Thrombomodulin (TM) is an endothelial cell membrane protein that acts as a major cofactor in the protein C anticoagulant pathway. The EGF-like domains 4–6 of TM (TM456) are essential for PC activation. In this study, we proposed a liposomal recombinant TM conjugate to mimic the membrane TM structure and its anticoagulant activity. First, a DSPE-PEG2000-TM456 was successfully synthesized by site-specific conjugation of azido-TM456 with DSPE-PEG2000-DBCO via copper-free click chemistry quantitatively. Then, liposome-TM456 was fabricated via direct liposome formation with the DSPE-PEG2000-TM456 and other lipids. This liposomal formulation of TM456 retained protein C activation activity as that of TM456. Also, liposome-TM456 was much more stable and had a longer plasma half-life than TM456 and DSPE-PEG2000-TM456, respectively. Moreover, liposome-TM456 showed in vivo anticoagulant effect by decreasing the mortality from 80% to 20% in a thrombin-induced thromboembolism mouse model. The reported liposome-TM456 conjugate mimics the endothelial TM anticoagulation activity and may serve as an effective anticoagulant agent candidate for future development.

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“…All the liposomes showed similar trend for the entrapment efficiency. The higher size of the maleimide functionalized liposomes may be due to vesicle aggregation (Loughrey et al, 1990).…”

Section: Discussionmentioning

confidence: 99%