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dc.contributor.authorAkdoğan, Yaşar
dc.contributor.authorEmrullahoğlu, Mustafa
dc.contributor.authorTatlıdil, Diğdem
dc.contributor.authorÜçüncü, Muhammed
dc.contributor.authorÇakan Akdoğan, Gülçin
dc.date.accessioned2017-07-17T11:05:10Z
dc.date.available2017-07-17T11:05:10Z
dc.date.issued2016
dc.identifier.citationAkdoğan, 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/c6cp04137jen_US
dc.identifier.issn1463-9076
dc.identifier.urihttp://doi.org/10.1039/c6cp04137j
dc.identifier.urihttp://hdl.handle.net/11147/5940
dc.description.abstractUnderstanding 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.en_US
dc.description.sponsorshipTurkish Scientific and Technological Research Council (2232-114C082)en_US
dc.language.isoengen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.isversionof10.1039/c6cp04137jen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBovine serum albuminen_US
dc.subjectElectron paramagnetic resonanceen_US
dc.subjectDrug deliveryen_US
dc.subjectSspin labelingen_US
dc.titleEPR studies of intermolecular interactions and competitive binding of drugs in a drug-BSA binding modelen_US
dc.typearticleen_US
dc.contributor.authorIDTR180857en_US
dc.contributor.authorIDTR203331en_US
dc.contributor.iztechauthorAkdoğan, Yaşar
dc.contributor.iztechauthorEmrullahoğlu, Mustafa
dc.contributor.iztechauthorTatlıdil, Diğdem
dc.contributor.iztechauthorÜçüncü, Muhammed
dc.relation.journalPhysical Chemistry Chemical Physicsen_US
dc.contributor.departmentİYTE, Mühendislik Fakültesi, Malzeme Bilimi ve Mühendisliği Bölümüen_US
dc.identifier.volume18en_US
dc.identifier.issue32en_US
dc.identifier.startpage22531en_US
dc.identifier.endpage22539en_US
dc.identifier.wosWOS:000381436500058
dc.identifier.scopusSCOPUS:2-s2.0-84981525021


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