Spectroscopic characterization of furosemide binding to human carbonic anhydrase II

International Journal of Biological Macromolecules
Samira RanjbarHoushang Nemati

Abstract

This study reports the interaction between furosemide and human carbonic anhydrase II (hCA II) using fluorescence, UV-vis and circular dichroism (CD) spectroscopy. Fluorescence data indicated that furosemide quenches the intrinsic fluorescence of the enzyme via a static mechanism and hydrogen bonding and van der Walls interactions play the major role in the drug binding. The binding average distance between furosemide and hCA II was estimated on the basis of the theory of Förster energy transfer. Decrease of protein surface hydrophobicity was also documented upon furosemide binding. Chemical modification of hCA II using N-bromosuccinimide indicated decrease of the number of accessible tryptophans in the presence of furosemide. CD results suggested the occurance of some alterations in α-helical content as well as tertiary structure of hCA II upon drug binding.

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Citations

Jan 21, 2015·International Journal of Biological Macromolecules·Ali KhatibiAli Akbar Moosavi-Movahedi
Apr 9, 2016·Pharmaceutical Development and Technology·Sara EsmaeilzadehParvin Zakeri-Milani
Jan 25, 2020·International Journal of Biological Macromolecules·Raziyeh GharibSusan Husseinzadeh

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