Spectroscopic characterization of furosemide binding to human carbonic anhydrase II.

Article Details

Citation

Ranjbar S, Ghobadi S, Khodarahmi R, Nemati H

Spectroscopic characterization of furosemide binding to human carbonic anhydrase II.

Int J Biol Macromol. 2012 May 1;50(4):910-7. doi: 10.1016/j.ijbiomac.2012.02.005. Epub 2012 Feb 16.

PubMed ID
22343084 [ View in PubMed
]
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 Forster 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 alpha-helical content as well as tertiary structure of hCA II upon drug binding.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
FurosemideCarbonic anhydrase 2ProteinHumans
No
Inhibitor
Details