Preparation and characterization of paramagnetic polychelates and their protein conjugates
Autor: | Alan D. Watson, Scott M. Rocklage, Paul F. Sieving |
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Rok vydání: | 1990 |
Předmět: |
Gadolinium DTPA
Gadolinium Biomedical Engineering Pharmaceutical Science chemistry.chemical_element Bioengineering Conjugated system Degree of polymerization Ligands chemistry.chemical_compound Heterocyclic Compounds Organometallic Compounds medicine Humans DOTA Polylysine Chelation Serum Albumin Chelating Agents Pharmacology Organic Chemistry Pentetic Acid Human serum albumin Monomer chemistry Indicators and Reagents Protein Binding Biotechnology Macromolecule Nuclear chemistry medicine.drug |
Zdroj: | Bioconjugate Chemistry. 1:65-71 |
ISSN: | 1520-4812 1043-1802 |
Popis: | The gadolinium complexes of poly-L-lysine-poly(diethylenetriamine-N,N,N',N",N"-pentaacetic acid) (Gd-PL-DTPA) and poly-L-lysine-poly(1,4,7,10-tetraazacyclododecane-N,N',N",N"'-tetr aacetic acid) (Gd-PL-DOTA) and their conjugates with human serum albumin (HSA) have been prepared and characterized. Poly-L-lysine (PL, degree of polymerization approximately 100) was N-acylated with a mixed anhydride of the chelating ligand (DTPA or DOTA). Sixty to ninety chelating groups per molecule of PL could be attached in this way. Following purification of the polychelate by size-exclusion chromatography, the gadolinium complexes were prepared by standard methods and conjugated to HSA with heterobifunctional cross-linking reagents. The molar relaxities of these macromolecular species were 2-3-fold higher than those of the corresponding monomeric metal complexes [( Gd(DTPA)] and [Gd(DOTA)]). The conjugation conditions were optimized to produce conjugates containing 60-90 metal centers per molecule of HSA (ca. one polychelate per protein). |
Databáze: | OpenAIRE |
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