Biophysical insight into the interaction of levocabastine with human serum albumin: spectroscopy and molecular docking approach

Abstract

Interaction of levocabastine with human serum albumin (HSA) is investigated by applying fluorescence spectroscopy, circular dichroism spectroscopy and molecular docking methods. Levocabastine is an important drug in treatment of allergy and currently a target drug for drug repurposing to treat other diseases like vernal keratoconjuctivitis. Fluorescence quenching data revealed that levocabastine bind weakly to protein with binding constant in the order of 10³ M⁻¹. Förster resonance energy transfer results indicated the binding distance of 2.28 nm for levocabastine. Synchronous fluorescence result suggest slight blue shift for tryptophan upon levocabastine binding, binding of levocabastine impelled rise in α-helical structure in protein, while there are minimal changes in tertiary structure in protein. Moreover, docking results indicate levocabastine binds to pocket near to the drug site-I in HSA via hydrogen bonding and hydrophobic interactions. Understanding the interaction of levocabastine with HSA is significant for the advancement of therapeutic and diagnostic strategies for optimal treatment results.

Communicated by Ramaswamy H. Sarma

Keywords:

• Circular dichroism spectroscopy
• fluorescence spectroscopy
• human serum albumin
• levocabastine
• molecular docking

Acknowledgements

Facilities provided by University of Tabuk are gratefully acknowledged. Authors extend their sincere thanks to Deanship of scientific Research at University of Tabuk for its funding of this research group no S-1440-0280.

Disclosure statement

The authors declare no competing interests.