Interaction of porphyrins with concanavalin A and pea lectin

Abstract

Currently porphyrins are used as photosensitizers in photodynamic therapy for the treatment of cancer. However, this approach suffers due to the inability of many porphyrin-based drugs to accumulate preferentially in tumours. In view of this, we considered if the carbohydrate-binding proteins, lectins, which preferentially recognize malignant cells, could be used for the targeting of porphyrins to tumour cells. In the present study, we have investigated the interaction of a free base porphyrin, meso-tetrasulphonatophenylporphyrin and the corresponding metal derivative, meso-zinc-tetrasulphonatophenylporphyrin with two legume lectins, concanavalin A and pea (Pisum sativum) lectin. Each lectin subunit was found to bind one porphyrin molecule and the association constant, Ka, estimated from absorption and fluorescence titrations at room temperature (28 ± 1°C) was in the range of 1.2 × 104 M-1 to 6.3 × 1044 M-1. Both free lectin and lectin saturated with the specific saccharide were found to bind the porphyrin with comparable binding strength, indicating that porphyrin binding takes place at a site different from the sugar-binding site. These results indicate that lectins may potentially serve as drug-delivery agents for porphyrin sensitizers in photodynamic therapy.