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Differences between Cu- and Fe–Cu nanoflowers in their interactions with fluorescent probes ANS and Fura-2 and proteins albumin and thrombin

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Abstract

Among nanomaterials, we can now distinguish a special class called nanoflowers (NFs). These new nanostructures have aroused the interest of scientists due to the topographic features of nanolayers, the special location which allows a higher surface-to-volume ratio compared to classical spherical nanoparticles, thereby significantly increasing the efficiency of surface reactions for nanoflowers. The main value of nanoflowers is their action as enzyme stabilizers. A protein stability is usually enhanced by immobilization on a nanoflower surface through charge affinity and covalent bonds. The possibility of their use in vivo in biocatalysis, biosensors and medicine has been also investigated. We now report on the synthesis of two different nanoflowers: Cu nanoflowers and Fe3+ attached Cu nanoflowers and their interaction with two fluorescent probes, anilino-1-naphthalenesulfonic acid (ANS) and Fura 2, and two proteins, human serum albumin (HSA) and thrombin. Nanoflowers did not bind ANS, but bind efficiently to Fura 2 and both proteins. Modification of Cu–NFs by Fe3+ leads to significant changes in their binding capacity to fluorescent probe Fura 2 and both proteins. Their ability to bind fluorescent probe Fura 2 increased eightfold, and their ability to bind HSA and thrombin increased five times. Regarding Fe3+–Cu–NFs, a difference in binding between HSA and thrombin was found that can be explained by their structural features. Our data indicate the possibility of using studied nanoflowers for sorption of fluorescent probes and proteins.

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Acknowledgements

This work was supported by the Technological Research Council of Turkey (TUBITAK) (Grant Number:118Z037) and by the State Committee of Science and Technology of Belarus and Belarussian Republican Foundation for Fundamental Research, grants B18TUB-001, B21TUB-001, B21KORG-001; by the Polish National Agency for Academic Exchange, grant EUROPARTNER, No. PPI/APM/2018/1/00007/U/001.

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Authors and Affiliations

  1. Institute of Biophysics and Cell Engineering, National Academy of Sciences of Belarus, Akademicheskaja 27, 220072, Minsk, Belarus

    Inessa Halets-Bui, Volha Dzmitruk, Viktar Abashkin, Svetlana Loznikova & Dzmitry Shcharbin

  2. Chemistry Dept. Biochemistry Division, Faculty of Arts and Science, Aksaray University, Aksaray, Turkey

    Ömür Acet, Burcu Önal & Mehmet Odabaşı

  3. Chemistry Dept. Biochemistry Division, Faculty of Science, Erciyes University, Kayseri, Turkey

    Nalan Özdemir

  4. Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland

    Maria Bryszewska

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  1. Inessa Halets-Bui
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Halets-Bui, I., Dzmitruk, V., Abashkin, V. et al. Differences between Cu- and Fe–Cu nanoflowers in their interactions with fluorescent probes ANS and Fura-2 and proteins albumin and thrombin. Polym. Bull. 79, 5247–5259 (2022). https://doi.org/10.1007/s00289-021-03773-z

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