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A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin

The interaction of pinostrobin (PS), a multitherapeutic agent with serum albumins of various mammalian species namely, goat, bovine, human, porcine, rabbit, sheep and dog was investigated using fluorescence quench titration and competitive drug displacement experiments. Analysis of the intrinsic flu...

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Detalles Bibliográficos
Autores principales: FEROZ, Shevin R., SUMI, Rumana A., MALEK, Sri N.A., TAYYAB, Saad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Japanese Association for Laboratory Animal Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427724/
https://www.ncbi.nlm.nih.gov/pubmed/25519455
http://dx.doi.org/10.1538/expanim.14-0053
Descripción
Sumario:The interaction of pinostrobin (PS), a multitherapeutic agent with serum albumins of various mammalian species namely, goat, bovine, human, porcine, rabbit, sheep and dog was investigated using fluorescence quench titration and competitive drug displacement experiments. Analysis of the intrinsic fluorescence quenching data revealed values of the association constant, K(a) in the range of 1.49 – 6.12 × 10(4) M(−1), with 1:1 binding stoichiometry. Based on the PS–albumin binding characteristics, these albumins were grouped into two classes. Ligand displacement studies using warfarin as the site I marker ligand correlated well with the binding data. Albumins from goat and bovine were found to be closely similar to human albumin on the basis of PS binding characteristics.