A New Approach to Determine Camptothecin and Its Analogues Affinity to Human Serum Albumin

• Published in: Journal of pharmaceutical sciences Vol. 100; no. 3; pp. 1142 - 1146
• Main Authors: Marszałł, Michał Piotr, Buciński, Adam, Kruszewski, Stefan, Ziomkowska, Blanka
• Format: Journal Article
• Language: English
• Published: Hoboken Elsevier Inc 01.03.2011; Wiley Subscription Services, Inc., A Wiley Company; Elsevier; Wiley; American Pharmaceutical Association; Elsevier Limited
• Subjects: analytical biochemistry; Antineoplastic Agents, Phytogenic - metabolism; Antineoplastic Agents, Phytogenic - pharmacokinetics; Biological and medical sciences; Blood Proteins - metabolism; Camptothecin - analogs & derivatives; Camptothecin - metabolism; Camptothecin - pharmacokinetics; cancer chemoprevention; Chemistry; Chemistry, Medicinal; Chemistry, Multidisciplinary; Drug Stability; General pharmacology; HPLC (high-performance/pressure liquid chromatography); Humans; kinetics; Life Sciences & Biomedicine; Ligands; Magnetics; Medical sciences; Pharmaceutical technology. Pharmaceutical industry; Pharmacology & Pharmacy; Pharmacology. Drug treatments; Physical Sciences; Protein Binding; Science & Technology; Serum Albumin - chemistry; Serum Albumin - metabolism; analytical biochemistry; cancer chemoprevention; protein binding; kinetics; HPLC (high-performance/pressure liquid chromatography); MEMBRANE; LIGAND; MAGNETIC NANOPARTICLES; PROTEINS; IMMOBILIZATION; Antineoplastic agent; Performance evaluation; Human; Pharmaceutical technology; Enzyme; HPLC (high-performance/ pressure liquid chromatography); DNA topoisomerase; Enzyme inhibitor; HPLC chromatography; Liquid chromatography; Serum albumin; Anticarcinogen; High pressure; Binding protein; Alkaloid; Isomerases; Affinity; Kinetics; Performance; Topoisomerase I inhibitor
• ISSN: 0022-3549; 1520-6017; 1520-6017
• DOI: 10.1002/jps.22318

A novel and fast method for the determination of the binding kinetic data of ligand to protein has been developed. A new tool including human serum albumin–coated magnetic beads (HSA-MB) was used to determine the affinity of camptothecin (CPT) and its analogues to HSA. From the biological activity point of view, these compounds have potential anticancer activity. However, the numerous studies indicate that some of these analogues have a strong affinity to plasma proteins stopping their effective therapy. Thus, the problem of plasma protein binding behavior of CPT's analogues was the subject of this study.