Spectroscopic characterization of furosemide binding to human carbonic anhydrase II

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• 作者：Samira Ranjbar^a ; Sirous Ghobadi^a ; ^{ghobadi@razi.ac.ir} ; ^{sirousghobadi@yahoo.com} ; Reza Khodarahmi^b ; Houshang Nemati^c
• 关键词：ANS ; 1-anilinonaphthalene-8-sulfonate ; CD ; circular dichroism ; hCA II ; human carbonic anhydrase II ; NBS ; N-bromosuccinimde ; PSH ; protein surface hydrophobicity ; SDS-PAGE ; sodium n-dodecyl sulfate-polyacrylamide gel electrophoresis
• 刊名：International Journal of Biological Macromolecules
• 出版年：2012
• 期刊代码：62_01418130
• 类别：abs
• 出版时间：1 May, 2012
• 卷：50
• 期：4
• 页码：910-917
• 文件大小：510 K

摘要

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 F枚rster 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 伪-helical content as well as tertiary structure of hCA II upon drug binding.