Interaction of Aggregated Cationic Porphyrins with Human Serum Albumin.

ABSTRACT: The interaction of an equilibrium mixture of monomeric and aggregated cationic trans-5,15-bis(N-methylpyridinium-4-yl)-10,15-bis-diphenylporphine (t-H₂Pagg) chloride salt with human serum albumin (HSA) has been investigated through UV/Vis absorption, fluorescence emission, circular dichroism and resonant light scattering techniques. The spectroscopic evidence reveals that both the monomeric t-H₂Pagg and its aggregates bind instantaneously to HSA, leading to the formation of a tight adduct in which the porphyrin is encapsulated within the protein scaffold (S₄₃₀) and to clusters of aggregated porphyrins in electrostatic interaction with the charged biomolecules. These latter species eventually interconvert into the final S_430<

SUBMITTER: Samperi M 

PROVIDER: S-EPMC9917112 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature