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The binding interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanine (AlPc), and two-serum albumins (bovine serum albumin (BSA) and human serum albumin (HSA)) has been investigated. AlPc could quench the intrinsic fluorescence of BSA and HSA through a static quenching process. The primary and secondary binding sites of AlPc on BSA were domain I and III of BSA. The primary binding site of AlPc on HSA was domain I, and the secondary binding sites of AlPc on HSA were found at domains I and II. Our results suggest that AlPc readily interact with BSA and HSA implying that the amphiphilic substituents AlPc may contribute to their transportation in the blood

journal of innovative optical health sciences/journal of innovation in optical health science

Spectroscopic analysis of the interaction between tetra-(<i>p</i>-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanines and serum albumins

Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanines and serum albumins