Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin
نویسندگان
چکیده
منابع مشابه
Spectroscopic, Thermodynamic and Molecular Docking Studies on Interaction of Toxic Azo Dye with Bovine Serum Albumin
Investigation on interaction of azo dyes with bovine serum albumin as carrier protein will be important in the field of toxicology because of distribution and transportation of dyes in blood. In this regard, the interaction between the azo dye, trisodium (4E)-3-oxo-4-[(4- sulfonato-1- naphthyl) hydrazono] naphthalene-2,7-disulfonate (C20H11N2Na3O10S3), known as Amaranth and bovine serum albumin...
متن کاملSpectroscopic, Docking and Molecular Dynamics Simulation Studies on the Interaction of Etofylline and Human Serum Albumin
The purpose of this study is to investigate the interaction of Etofylline as an established drug for asthma remedy, with the major transport protein in human blood circulation, the human serum albumin (HSA). In this respect, the fluorescence and circular dichroism (CD) spectroscopy techniques, along with the molecular docking and molecular dynamics simulation methods were employed. Analysis of ...
متن کاملInteraction of Phthalocyanine with Egg albumin and Bovine serum albumin
The interaction of bovine serum albumin ( BSA) and egg albumin with water solublephthalocyanine, cobalt (ΙΙ) 4, 4′ , 4′′, 4′′′- tetrasulfophthalocyanine ( CoTSPc) , has been studiedby the UV- Vis method at pH 7.0 and five different temperatures 20, 25, 30, 35 and 40°C. Theformation constants have been elucidated by using spectrophotometric titration and computerSQUAD program data refinement. Th...
متن کاملSpectroscopic Study of Dipicolinic Acid Interaction with Bovine Serum Albumin
Spectral changes of bovine serum albumin (BSA) in the presence of dipicolinic acid (DPA) were studied with UV/Vis absorption and fluorescence spectroscopy. The change in UV/vis spectra of BSA in the presence of DPA indicated the protein weakly interacting with DPA. The DPA quenching to the fluorescence of BSA leads to the calculation of the BAS-DPA association constant K of 8.9 x 104 Lmol-1 at ...
متن کاملSpectroscopic studies on the interaction between erlotinib hydrochloride and bovine serum albumin
BACKGROUND AND THE PURPOSE OF THE STUDY The binding ability of a drug to serum albumin has influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of anticancer drug erlotinib hydrochloride with bovine serum albumin (BSA) using fluorescence and UV/vis spectroscopy was investigated. METHODS The BSA solution (0.1 mM) was prepared daily in Tris buffer (0.05 mol ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Pharmaceutica Sinica B
سال: 2012
ISSN: 2211-3835
DOI: 10.1016/j.apsb.2011.12.001