Jana Staničová1,2, Valéria Verebová3, Jiří Beneš2. 1. Institute of Biophysics, University of Veterinary Medicine & Pharmacy, Košice, Slovakia jana.stanicova@uvlf.sk. 2. Institute of Biophysics & Informatics, First Faculty of Medicine, Charles University, Prague, Czech Republic. 3. Institute of Biophysics, University of Veterinary Medicine & Pharmacy, Košice, Slovakia.
Abstract
BACKGROUND/AIM: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. MATERIALS AND METHODS: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. RESULTS: The strength of interaction expressed by binding constants was found to be 4.0×104 l/mol for hypericin-DNA and 8.1×104 l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. CONCLUSION: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate. Copyright
BACKGROUND/AIM: We report the incorporation of prospective anticancer agent hypericin into DNA and bovineserum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. MATERIALS AND METHODS: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. RESULTS: The strength of interaction expressed by binding constants was found to be 4.0×104 l/mol for hypericin-DNA and 8.1×104 l/mol for emodin-DNA complex. Both molecules stabilize bovineserum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. CONCLUSION: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovineserum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate. Copyright
Authors: A A Moosavi-Movahedi; A K Bordbar; A A Taleshi; H M Naderimanesh; P Ghadam Journal: Int J Biochem Cell Biol Date: 1996-09 Impact factor: 5.085
Authors: J Radovic; D Maksimovic-Ivanic; G Timotijevic; S Popadic; Z Ramic; V Trajkovic; D Miljkovic; S Stosic-Grujicic; S Mijatovic Journal: Food Chem Toxicol Date: 2012-06-07 Impact factor: 6.023