Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5940
Title: EPR studies of intermolecular interactions and competitive binding of drugs in a drug-BSA binding model
Authors: Akdoğan, Yaşar
Emrullahoğlu, Mustafa
Tatlıdil, Diğdem
Üçüncü, Muhammed
Çakan Akdoğan, Gülçin
Keywords: Bovine serum albumin
Electron paramagnetic resonance
Drug delivery
Sspin labeling
Issue Date: 2016
Publisher: Royal Society of Chemistry
Source: Akdoğan, Y., Emrullahoğlu, M., Tatlıdil, D., Üçüncü, M., and Çakan Akdoğan, G. (2016). EPR studies of intermolecular interactions and competitive binding of drugs in a drug-BSA binding model. Physical Chemistry Chemical Physics, 18(32), 22531-22539. doi:10.1039/c6cp04137j
Abstract: Understanding intermolecular interactions between drugs and proteins is very important in drug delivery studies. Here, we studied different binding interactions between salicylic acid and bovine serum albumin (BSA) using electron paramagnetic resonance (EPR) spectroscopy. Salicylic acid was labeled with a stable radical (spin label) in order to monitor its mobilized (free) or immobilized (bound to BSA) states. In addition to spin labeled salicylic acid (SL-salicylic acid), its derivatives including SL-benzoic acid, SL-phenol, SL-benzene, SL-cyclohexane and SL-hexane were synthesized to reveal the effects of various drug binding interactions. EPR results of these SL-molecules showed that hydrophobic interaction is the main driving force. Whereas each of the two functional groups (-COOH and -OH) on the benzene ring has a minute but detectable effect on the drug-protein complex formation. In order to investigate the effect of electrostatic interaction on drug binding, cationic BSA (cBSA) was synthesized, altering the negative net charge of BSA to positive. The salicylic acid loading capacity of cBSA is significantly higher compared to that of BSA, indicating the importance of electrostatic interaction in drug binding. Moreover, the competitive binding properties of salicylic acid, ibuprofen and aspirin to BSA were studied. The combined EPR results of SL-salicylic acid/ibuprofen and SL-ibuprofen/salicylic acid showed that ibuprofen is able to replace up to ∼83% of bound SL-salicylic acid, and salicylic acid can replace only ∼14% of the bound SL-ibuprofen. This indicates that ∼97% of all salicylic acid and ibuprofen binding sites are shared. On the other hand, aspirin replaces only ∼23% of bound SL-salicylic acid, and salicylic acid replaces ∼50% of bound SL-aspirin, indicating that ∼73% of all salicylic acid and aspirin binding sites are shared. These results show that EPR spectroscopy in combination with the spin labeling technique is a very powerful method to investigate drug binding dynamics in detail.
URI: http://doi.org/10.1039/c6cp04137j
http://hdl.handle.net/11147/5940
ISSN: 1463-9076
1463-9084
1463-9076
Appears in Collections:Chemistry / Kimya
Materials Science and Engineering / Malzeme Bilimi ve Mühendisliği
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

Files in This Item:
File Description SizeFormat 
5940.pdfMakale2.24 MBAdobe PDFThumbnail
View/Open
Show full item record

CORE Recommender

SCOPUSTM   
Citations

18
checked on Dec 4, 2021

WEB OF SCIENCETM
Citations

16
checked on Dec 4, 2021

Page view(s)

36
checked on Dec 8, 2021

Download(s)

30
checked on Dec 8, 2021

Google ScholarTM

Check

Altmetric


Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.