Published January 1, 2022 | Version v1
Journal article Open

First protein affinity application of Cu2+-bound pure inorganic nanoflowers

  • 1. Aksaray Univ, Fac Arts & Sci, Biochem Div, Chem Dept, TR-68100 Aksaray, Turkey
  • 2. Tarsus Univ, Vocat Sch Hlth Sci, Pharm Serv Program, Tarsus, Turkey
  • 3. Natl Acad Sci Belarus, Inst Biophys & Cell Engn, Minsk, BELARUS
  • 4. Erciyes Univ, Biochem Div, Chem Dept, Fac Sci, TR-38030 Kayseri, Turkey

Description

Today, a new kind of materials is introduced to separation media day by day to increase the efficiency of the separation processes, and multiple-petalled nanostructured materials are one of them. In this study, new pure inorganic copper phosphate nanoflowers (pCP-NFs) were synthesized, and some environmental conditions affecting on binding mechanism with human serum albumin were evaluated via changing medium pH, temperature, initial human serum albumin (HSA) amount and salt concentrations. Before experimental studies, pCP-NFs were subjected to some characterization tests such as scanning electron microscopy, energy-dispersive X-ray, X-ray diffraction and Fourier transform infrared spectroscopy. Besides a lot of valuable instrumental data, some obtained experimental ones as follows: after Cu2+ ions attachment to pCP-NFs as ligand, maximum HSA adsorption capacity of obtained Cu2+-pCP-NFs was found as 225.7 mg/g with an initial concentration of 1.5 mg/mL at pH 7 and 25 degrees C. Langmuir and Freundlich adsorption equations were evaluated for determination of appropriate adsorption model in interaction, and Langmuir model found as the fittest one with a R-2 of 0.9949 was also reviewed to determine Gibbs free energy between HSA and Cu2+-pCP-NFs interaction.

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