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Removal of endotoxin in blood by polymyxin B immobilized polystyrene-derivative fiber
Kazuo Teramoto1, Yoshiaki Nakamoto, Tetsunosuke Kunitomo
1Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan.
Abstract:
Polymyxin B, a cationic cyclic decapeptide antibiotic, is well known to bind endotoxin and to neutralize its toxicity. Based on this principle, polymyxin B was immobilized on the chloroacetamidomethylated polystyrene fiber that is reinforced by polypropylene. The adsorbing capacity of the obtained fibers (polymyxin B immobilized fiber [PMX-F]) was evaluated on endotoxin and other serum components in serum and on heparin in phosphate-buffered saline. Fluorescein isothiocyanate-labeled or tetramethylrhodamine isothiocyanate-labeled lipopolysaccharide (LPS) was used as endotoxin. The measurement of the fluorescence intensity showed that PMX-F adsorbed these LPSs depending on their concentration and on amount. The adsorption of endotoxin was confirmed by desorption of LPS from PMX-F as well. PMX-F adsorbed serum amyloid protein A besides LPS, but neither C-reactive protein nor low-density lipoprotein. The adsorbing property of heparin was low.
Insights
Polymyxin B immobilized fibers (PMX-F) effectively adsorb endotoxins (lipopolysaccharide) from serum. This novel material also binds serum amyloid protein A, showing potential for targeted adsorption applications.
Area of Science:
- Biomaterials Science
- Medical Chemistry
- Biotechnology
Background:
- Polymyxin B is a cyclic decapeptide antibiotic known for its endotoxin-binding and toxicity-neutralizing properties.
- Immobilizing bioactive molecules onto solid supports is a key strategy in developing advanced medical materials.
- Endotoxins, particularly lipopolysaccharides (LPS), are potent pyrogens that pose significant risks in medical settings.
Purpose of the Study:
- To develop and characterize a novel fiber material for endotoxin adsorption.
- To evaluate the adsorption capacity of polymyxin B immobilized fibers (PMX-F) for lipopolysaccharide (LPS) and other serum components.
- To assess the binding affinity of PMX-F for heparin.
Main Methods:
- Polymyxin B was immobilized onto chloroacetamidomethylated polystyrene fiber reinforced with polypropylene.
- The adsorption capacity of the resulting PMX-F was tested using fluorescein or tetramethylrhodamine-labeled lipopolysaccharide (LPS) in serum.
- Adsorption was quantified by measuring fluorescence intensity and confirmed through desorption studies.
- Binding of other serum components like serum amyloid protein A, C-reactive protein, low-density lipoprotein, and heparin was also evaluated.
Main Results:
- PMX-F demonstrated significant adsorption of labeled LPS, with capacity dependent on LPS concentration and fiber amount.
- Confirmation of endotoxin adsorption was achieved through successful desorption of LPS from the PMX-F.
- PMX-F effectively adsorbed serum amyloid protein A but showed minimal binding to C-reactive protein and low-density lipoprotein.
- The adsorption of heparin by PMX-F was found to be low.
Conclusions:
- Polymyxin B immobilized fibers (PMX-F) represent an effective adsorbent for endotoxins (LPS).
- PMX-F exhibits selective adsorption, binding LPS and serum amyloid protein A while largely excluding other tested serum proteins.
- The developed PMX-F material shows promise for applications requiring the removal of endotoxins and potentially other specific biomolecules from biological fluids.
