Abstract
Interaction of xanthine oxidase (XOD), a key enzyme in purine metabolism, with cetyltrimethylammonium bromide (CTAB) and bis(cetyldimethylammonium)hexane dibromide (C16C6C16Br2) has been studied by employing different techniques at pH 7.4 and 25 °C. The existence of interaction between the surfactants and the enzyme was established by the deviation of tensiometric profiles of surfactants with and without the enzyme. The results obtained by Circular Dichroism, Fluorescence and activity suggest that the Gemini surfactant interacts strongly with the XOD than its conventional homologue. The peculiar structural design of C16C6C16Br2, enhanced ability for electrostatic and hydrophobic interactions, and unique aggregation behavior is accountable for the effectiveness of the Gemini in interacting/unfolding the XOD. The results are contemplated to offer valuable understandings in designing the surfactant-based formulations to moderate the activity of XOD.
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