Biophysical Characterization of the Interaction between a Transport Human Plasma Protein and the 5,10,15,20-Tetra(pyridine-4-yl)porphyrin.

ABSTRACT: The interaction between human serum albumin (HSA) and the non-charged synthetic photosensitizer 5,10,15,20-tetra(pyridine-4-yl)porphyrin (4-TPyP) was evaluated by in vitro assays under physiological conditions using spectroscopic techniques (UV-vis, circular dichroism, steady-state, time-resolved, synchronous, and 3D-fluorescence) combined with in silico calculations by molecular docking. The UV-vis and steady-state fluorescence parameters indicated a ground-state association between HSA and 4-TPyP and the absence of any dynamic fluorescence quenching was confirmed by the same average fluorescence lifetime for HSA without (4.76 ± 0.11 ns) and with 4-TPyP (4.79 ± 0.14 ns). Therefore, the Stern-Volmer quenching (K_SV) constant reflects the binding affinity, indicating a mode

SUBMITTER: Chaves OA 

PROVIDER: S-EPMC9413328 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature