Interaction studies of diazacyclam-based macrocyclic copper complex with bovine serum albumin (BSA): Spectroscopic investigations

سال انتشار: 1396
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 431

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شناسه ملی سند علمی:

NRCP03_010

تاریخ نمایه سازی: 21 اردیبهشت 1397

چکیده مقاله:

In the present investigation, the interaction of a new macrocyclic copper(II) complex, [CuL]Br2, that L is 1,3,6,10,12,15-hexa aza tricyclo [13.3.1.16,10] eicosane with the transportprotein, bovine serum albumin (BSA), was studied in vitro under simulated physiologicalconditions using multi-spectroscopic methods. It is found that [CuL]Br2 has a strong ability toquench the intrinsic fluorescence of BSA through static quenching mechanism with a bindingconstant of about 104 M-1. Thermodynamic parameters (ΔH < 0 and ΔS < 0) and competitivefluorescence study with ANS, indicated that van der Waals force and hydrogen bonding playmajor roles in the binding of complex and BSA. Job’s plot result confirms that there is onebinding site in BSA for Cu(II) complex (1:1 stoichiometry). The displacement experiments indicate that the binding of [CuL]Br2 to BSA primarily occurred in the sub-domain IIA (siteI) of BSA. The results of circular dichroism (CD) and UV–vis spectroscopy showed that themicroenvironment of amino acid residues and the conformation of BSA were changed afteraddition of [CuL]Br2 complex.

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نویسندگان

Nahid Shahabadi

Department of Chemistry, Faculty of Science, Razi University, Kermanshah, Iran

Mohammad Hakimi

Medical Biology Research Center (MBRC) Kermanshah University of Medical Sciences, Kermanshah, Iran

Teimoor Morovati

Department of Chemistry, Payame Noor University, ۱۹۳۹۵-۴۶۹۷ Tehran, Iran