Abstract
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.
Highlights
Photodynamic therapy (PDT) is a noninvasive treatment modality for several diseases, such as solid cancers,[1] port wine stains,[2] wet age-related macular degeneration (AMD)[3] and so on
The results suggested that the added bovine serum albumin (BSA) and human serum albumin (HSA) result in monomerization of the aluminum (III) phthalocyanine (AlPc)
The primary and secondary binding sites of AlPc to BSA were on domains I and III of BSA
Summary
Photodynamic therapy (PDT) is a noninvasive treatment modality for several diseases, such as solid cancers,[1] port wine stains,[2] wet age-related macular degeneration (AMD)[3] and so on. PDT treatment evolved utilizing an appropriate light This is an Open Access article published by World Scientic Publishing Company. Many photosensitizers have been reported for their potential of application in PDT, such as photofrin, hematoporphyrin derivatives, 5-aminolevulinic acid (ALA) and silicon phthalocyanine (Pc4),[6,7,8] so far there are only a few photosensitizers under clinical applications. It might be the results of hydrophobia and poor photophysical and physicochemical properties of these photosensitizers. New photosensitizers with better hydrophilia property and excellent photophysical and physicochemical properties are in great demand
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