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Biomedical subjects

T Blunk

Publications and source records attributed to T Blunk.

23 records · Page 2Linked to original sources
PubMed1997

The influence of the sample preparation on plasma protein adsorption patterns on polysaccharide-stabilized iron oxide particles and N-terminal microsequencing of unknown proteins.

The in vivo organ distribution of i.v. injected drug carriers is strongly influenced by the adsorption of plasma proteins after i.v. injection, e.g. uptake by the mononuclear phagocytic system (MPS). 2-D PAGE could be established to analyze plasma protein adsorption patterns on polysaccharide-stabilized aqueous iron oxide dispersions used as contrast agents in Magnetic Resonance Imaging (MRI). After incubation in human plasma, centrifugation, a washing procedure and a solubilization step were carried out to obtain the proteins adsorbed onto these ultrasmall particles (65 nm in diameter). Patterns of adsorbed proteins were analyzed in dependence on the washing medium used, i.e. highly purified water, phosphate buffered saline and Krebs buffer pH 7.4. Conductivity and composition of the washing medium influenced the adsorption of IgG onto the particles, but had little effect on the other proteins present. IgG was strongly reduced when using the relatively high conductive buffers. The more stabilizing polysaccharide was desorbed the larger was the total amount of adsorbed proteins. Appearance of two unknown chains of spots in the range of appr. 92 kDa, accounting for appr. 10% and 2% of the overall detected protein amount, was observed only when using Krebs buffer during the washing process. Performing N-terminal microsequencing one unknown chain of spots could be identified as a dimer of fibrinogen gamma chains.

Adsorption↗
PubMed1996

Fat emulsions based on structured lipids (1,3-specific triglycerides): an investigation of the in vitro interaction with plasma proteins.

Structured lipids (1,3-specific triglycerides) are new chemical entities made by enzymatic transesterification of the fatty acids in the 1,3-positions of the triglyceride. The purpose of this study was to investigate the in vitro interaction of fat emulsions based on either structured lipids or vegetable oils with human plasma proteins employing two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The structured lipids are triglycerides of the SLS and MLM types, where S is short-chain fatty acids (C4), M is medium-chain fatty acids (C8-10) and L is long-chain fatty acids (C16-18). The vegetable oil-based fat emulsions were the commercially available product, Intralipid, and a soybean oil (LLL) emulsion made de novo identically as the emulsions containing structured lipids. The SLS emulsion was found to adsorb a different protein pattern than the MLM and LLL emulsions. The protein pattern of the SLS emulsion was similar to the protein pattern of Intralipid. These findings might explain the in vivo difference in elimination found in another study, where the emulsion based on structured lipids with short-chain fatty acids in the 1,3-positions was removed more slowly from the general blood circulation compared to emulsions based on lipids with long-chain fatty acids in the 1,3-positions (LLL).

Journal Article↗
PubMed1993

Colloidal carriers for intravenous drug targeting: plasma protein adsorption patterns on surface-modified latex particles evaluated by two-dimensional polyacrylamide gel electrophoresis.

Targeting to specific sites of the body via colloidal carriers is sought in order to reduce drug side effects. The adsorption of plasma proteins on intravenously injected particles is regarded as the key factor in explaining their organ distribution: total bound protein, or, more likely, the presence of specific proteins and their conformation, are expected to influence macrophage uptake. Polystyrene beads, 60 nm in diameter, were used as model carriers; their surface was differentially modified by adsorption of increasingly hydrophilic block copolymers, poloxamers 184, 188 and 407. After incubation in plasma, the patterns of protein adsorption onto coated beads were analyzed by high-resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The behavior of some representative proteins was monitored, including albumin, fibrinogen, IgG, factor B and the apolipoproteins, A-I, A-IV, C-III, E and J. The more hydrophobic the particles, the larger the total amount of bound protein. However, this correlation was not valid for all of the analyzed protein species, which proves that it is insufficient to look only at physicochemical data to predict organ distribution. On the contrary, it is essential to use 2-D PAGE to establish the correlation between adsorbed proteins and carrier behavior in vivo.

Adsorption↗