Nonlinear van't Hoff Behavior in the Interaction of Two Water-Soluble Porphyrins with Bovine Serum Albumin (BSA).

ABSTRACT: Thermodynamic analysis of the binding process of water-soluble negatively charged meso-tetrakis(p-sulfonatophenyl) (TPPS₄) and positively charged meso-tetrakis(4-methylpyridyl) (TMPyP) porphyrins with bovine serum albumin (BSA) at different temperatures was carried out based on the data of BSA quenching fluorescence by porphyrins. The comparison of binding constants (K _b) shows that negatively charged TPPS₄ possesses higher affinity to BSA than positively charged TMPyP. Thermodynamic characteristics of the binding process were obtained in accordance with the van't Hoff theory by processing nonlinear dependences of ln K _b on inverse absolute temperature within the framework of two models: taking into account the

SUBMITTER: Bezerra FC 

PROVIDER: S-EPMC11618399 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature