Dissection of the interaction between human holo-transferrin and ciprofloxacin in the presence of silver nanoparticles: spectroscopic approaches
Autor: | Maryam Kamshad, Fatemeh Koohzad, Sima Beigoli, Jamshidkhan Chamani, Mahtab JahanShah-Talab, Reza Assaran Darban |
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Rok vydání: | 2017 |
Předmět: |
Holo transferrin
Circular dichroism Quenching (fluorescence) Chemistry 02 engineering and technology Cell Biology Plant Science 010402 general chemistry 021001 nanoscience & nanotechnology Resonance (chemistry) 01 natural sciences Biochemistry Silver nanoparticle 0104 chemical sciences Genetics Animal Science and Zoology Binding site 0210 nano-technology Ternary operation Molecular Biology Protein secondary structure Ecology Evolution Behavior and Systematics Nuclear chemistry |
Zdroj: | Biologia. 72:569-580 |
ISSN: | 1336-9563 0006-3088 |
Popis: | The binding of ciprofloxacin (CIP) to human holo-transferrin (HTF) in the presence of silver nanoparticles (AgNPs) has been investigated by fluorescence quenching and circular dichroism (CD) techniques as well as resonance light scattering under physiological conditions. It was determined that the intrinsic fluorescence of HTF was quenched by CIP in the presence of AgNPs through static quenching, thus confirming that a CIP-HTF complex was formed in both the binary and ternary systems. However, the analysis of HTF fluorescence quenching in these binary and ternary systems indicated that the AgNPs were affected upon complex formation between CIP and HTF and that the binding affinity between them became more substantial when the AgNPs coexisted with the drug. Fluorescence quenching proved that HTF had one class of binding sites for CIP in both binary and ternary systems. CD spectra indicated that the secondary structure of HTF changed when increasing the CIP concentration and during the simultaneous presence of CIP and AgNPs, which led to decreased contents of α-helix and β-sheet structures in HTF, inducing destabilization of the protein. |
Databáze: | OpenAIRE |
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