Photophysical, photochemical and bovine serum albumin binding studies on water-soluble gallium(III) phthalocyanine derivatives

2007 ◽  
Vol 11 (09) ◽  
pp. 635-644 ◽  
Author(s):  
Abimbola Ogunsipe ◽  
Tebello Nyokong ◽  
Mahmut Durmuş
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Water Soluble ◽  
Albumin Binding ◽  
Binding Studies ◽  
Amphiphilic Compounds ◽  
Yield Values ◽  
Bovine Serum Albumin Binding

Spectral, photophysical, photochemical and bovine serum albumin binding studies on some gallium(III) derivatives - {1,(4)-(tetrapyridyloxyphthalocyaninato)gallium(III), (α GaPc ); 2,(3)-(tetrapyridyloxyphthalocyaninato)gallium(III), (β GaPc ); and their quaternized derivatives: Q α GaPc and Q β GaPc )} are hereby presented. β-Substituted complexes are more fluorescent, but show lower tendencies to undergo intersystem crossing than the α-substituted, as judged by their fluorescence and triplet quantum yield values. The quaternized derivatives ( QGaPc ) are water-soluble and non-aggregated, which makes them potential photosensitizers of choice for photodynamic therapy applications; these amphiphilic compounds also bind strongly to bovine serum albumin in 1:1 stoichiometries, and with binding constants ( Kb) in the order of 106M−1.

Complexes of bovine serum albumin with water-soluble Cu and Co containing cationic meso-tetra(4-N-oxyethylpyridyl)-porphyrins

2007 ◽  
Vol 11 (07) ◽  
pp. 475-480 ◽  
Author(s):  
Nelli H. Karapetyan ◽  
Lusine R. Aloyan ◽  
Robert K. Ghazaryan ◽  
Yevgeni Mamasakhlisov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Visible Region ◽  
Binding Constants ◽  
Water Soluble ◽  
Albumin Binding ◽  
Binding Isotherms ◽  
Bovine Serum Albumin Binding ◽  
Scatchard Plots

Bovine serum albumin complexes with water-soluble cationic porphyrins, Cu - and Co-meso-tetra(4- N -hydroxyethylpyridyl)porphyrins ( CuT4OEPyP , CoT4OEPyP ), and their 3- N -analogs, meso-tetra(3- N -hydroxyethylpyridyl)porphyrins ( CuT3OEPyP , CoT3OEPyP ), have been investigated. The porphyrin-bovine serum albumin binding was monitored by the absorption in the visible region at 400-460 nm. The stoichiometry of binding and the binding constants of the porphyrins to bovine serum albumin were determined using binding isotherms and Scatchard plots. The K b values obtained for these porphyrin- bovine serum albumin complexes are 1.7 × 105 M −1, 3.2 × 105 M −1, 1.4 × 105 M −1 and 3 × 105 M −1 respectively. Binding constants are sensitive to pH and ionic strength of the solution.

Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd(II) complex incorporating 2,2′-(propane-1,3-diyl)bis(1H-imidazole-4,5-dicarboxylate)

2019 ◽  
Vol 44 (3-4) ◽  
pp. 198-205 ◽  
Author(s):  
Xiao-Fei Li ◽  
Li-Gang Ma ◽  
Yan-Qiu Yang ◽  
Yan-Ju Liu ◽  
Xiang-Ru Meng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Entropy Change ◽  
Chain Structure ◽  
Binding Studies ◽  
Carboxylate Oxygen ◽  
Fluorescence Measurements ◽  
Bovine Serum Albumin Binding

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.

Spectrofluorimetric study of finasteride and bovine serum albumin interaction and its application for quantitative determination of finasteride in tablet dosage form

2015 ◽  
Vol 7 (12) ◽  
pp. 5096-5102 ◽  
Author(s):  
Ali Saber Abdelhameed ◽  
Amer M. Alanazi ◽  
Adnan A. Kadi
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Quantitative Determination ◽  
Bovine Serum ◽  
Dosage Form ◽  
Albumin Binding ◽  
Bovine Serum Albumin Binding ◽  
Tablet Dosage ◽  
Accurate Quantification

Finasteride and bovine serum albumin binding is investigated and used for simple, accurate quantification of finasteride in tablets.

Bovine serum albumin binding, antioxidant and anticancer properties of an oxidovanadium(IV) complex with luteolin

2016 ◽  
Vol 157 ◽  
pp. 80-93 ◽  
Author(s):  
Luciana G. Naso ◽  
Luis Lezama ◽  
María Valcarcel ◽  
Clarisa Salado ◽  
Patricia Villacé ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Albumin Binding ◽  
Anticancer Properties ◽  
Bovine Serum Albumin Binding
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