Dissociation of the DCF-Hb complex in presence of cationic micelles: A spectroscopic and computational approach

Diclofenac sodium (DCF) is a derivative of phenyl acetic acid and a model representative of the family of non-steroidal anti-inflammatory drugs (NSAIDs). It is extensively consumed for treating inflammation and degenerative disorders like rheumatoid arthritis. The micelles or aggregates of surfactants have ability to solubilize poorly soluble drugs thereby increasing bioavailability of the drugs. Thus, in the current study we have shown a systematic approach for the association of diclofenac with haemoglobin and deintercalation of DCF from hemoglobin (Hb) by hexadecyltrimethylammonium bromide (CTAB) micelles by using various spectroscopic techniques. The fluorescence and UV-visible spectral results revealed that DCF interacts with CTAB micelles and resides in its hydrophobic core. Thus, steady fluorescence and UV-visible measurements provides a strong sign for the relocation of DCF molecules from the hemoglobin interior to the micellar interface of CTAB above cmc. The CD results hinted that CTAB micelles do not disturb the structure of hemoglobin, which further supported that CTAB micelles can be applied as a reliable delivery vehicle for DCF. The present study may be significant for the discovery of improved micelle-based vehicles to the delivery of non-steroidal anti-inflammatory drugs in their targeted site. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study demonstrates a systematic method for associating diclofenac with hemoglobin and removing DCF from hemoglobin by CTAB micelles. DCF interacts with CTAB micelles and resides in its hydrophobic core according to fluorescence and UV-visible spectral results. CD results suggest that CTAB micelles do not disrupt the structure of hemoglobin, supporting their use as a reliable delivery vehicle for DCF.