Dergi makalesi Açık Erişim
Akbay, Nuriye; Tok, Tugba Taskin; Seferoglu, Zeynel; Gokoglu, Elmas
<?xml version='1.0' encoding='utf-8'?> <oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd"> <dc:creator>Akbay, Nuriye</dc:creator> <dc:creator>Tok, Tugba Taskin</dc:creator> <dc:creator>Seferoglu, Zeynel</dc:creator> <dc:creator>Gokoglu, Elmas</dc:creator> <dc:date>2018-01-01</dc:date> <dc:description>The interaction mechanisms of two ethidium derivatives, 3,8-dibenzoylamino-5-ethyl-6-phenylphenantridinium chloride (E2) and 3,8-diphenylacetylamino-5-ethyl-6-phenylphenantridinium chloride (E3) with serum albumins (BSA and HSA) have been investigated by a combined experimental and computational approach. Fluorescence quenching and UV-vis results revealed that the interaction of derivatives with albumins resulted in formation of ground-state complexes and the obtained Stern-Volmer quenching constants designate the presence of a static component in the quenching mechanisms. Thermodynamic parameters (H and S values) point out the ionic interactions play the major role in E2-BSA, E2-HSA and E3-HSA complexes. The van der Waals interactions are dominant forces in E3-BSA complex. Moreover, the obtained results in this study were supported with computational analyzes which have same tendency.</dc:description> <dc:identifier>https://aperta.ulakbim.gov.trrecord/33043</dc:identifier> <dc:identifier>oai:zenodo.org:33043</dc:identifier> <dc:rights>info:eu-repo/semantics/openAccess</dc:rights> <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights> <dc:source>JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS 36(12) 3114-3121</dc:source> <dc:title>Investigation of binding properties of two ethidium derivatives with serum albumins: spectral and computational approach</dc:title> <dc:type>info:eu-repo/semantics/article</dc:type> <dc:type>publication-article</dc:type> </oai_dc:dc>
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