Spectroscopic and molecular modeling of the binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin

Photooxidation of lysozyme or serum albumin bound to meso-tetra-arylporphyrins

“…The available data concerning THPP refer to HSA, where n ¼ 1 and K d1 ¼ 0.7 mM and K d2 ¼ 4 mM at pH 7 and K d is ca. 7-fold lower at pH 3 [21]. Table 3 are in agreement with the better binding of the diprotonated dye.…”

“…a stretch of polypeptide chain with backbone in an almost fully extended conformation, are absent. The main driving force for the binding of THPP to HSA has been ascribed to hydrophobic domains and the induced conformational change reduces the number of a-helices in the albumin [21].…”

“…Binding of THPP to BSA has recently been studied at several pH values [21]. Lysozyme is one of the best understood small enzymes, its activity can be readily monitored and it has specific binding sites, one of which is surrounded by four tryptophan residues [37e40].…”

Thermodynamic Aspects of Binding Proteins with Porphyrins. Spectral and Thermochemical Approaches

“…The mechanism of fluorescence quenching was determined by Stern-Volmer approach. [11] The thermodynamic characteristics were determined by the Van't Hoff equation. [12] Molecular complex formation of the studied porphyrins with BSA was studied by isothermal titration calorimetry using a differential automatic titration calorimeter.…”

Photoprocesses of chlorin e6 bound to lysozyme or bovin serum albumin

“…Another class of photosensitizers is constituted by the porphyrin moiety [28][29][30][31][32][33][34][35][36][37][38][39][40][41]. The amount of knowledge about chlorins is much smaller than about porphyrins and only little is available in the literature concerning chlorin-sensitized photooxidation of proteins.…”