Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform
The interactions between proteins and nanoparticles need to be fully characterized as the immobilization of proteins onto various nanoplatforms in the physiological system often results in the change of surface of the protein molecules to avoid any detrimental issues related to their biomedical appl...
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MDPI AG
2021-07-01
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Online Access: | https://www.mdpi.com/2227-9059/9/8/858 |
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author | Atanu Naskar Sohee Lee Dongjoon Ko Semi Kim Kwang-sun Kim |
author_facet | Atanu Naskar Sohee Lee Dongjoon Ko Semi Kim Kwang-sun Kim |
author_sort | Atanu Naskar |
collection | DOAJ |
description | The interactions between proteins and nanoparticles need to be fully characterized as the immobilization of proteins onto various nanoplatforms in the physiological system often results in the change of surface of the protein molecules to avoid any detrimental issues related to their biomedical applications. Hence, in this article, the successful low-temperature synthesis of a BP-based γ-Fe<sub>2</sub>O<sub>3</sub> (IB) nanocomposite and its interactive behavior with bovine serum albumin (BSA)—a molecule with chemical similarity and high sequence identity to human serum albumin—are described. To confirm the formation of γ-Fe<sub>2</sub>O<sub>3</sub> and the IB nanocomposite, X-ray diffraction, transmission electron microscopy, and X-ray photoelectron spectroscopy analyses of the materials were performed. Additionally, the physical interaction between BSA and the IB nanocomposite was confirmed via UV–Vis and photoluminescence spectral analyses. Finally, the biocompatibility of the BSA-immobilized IB nanocomposite was verified using an in vitro cytotoxicity assay with HCT-15 colon cancer cells. Our findings demonstrate that this newly developed nanocomposite has potential utility as a biocompatible nanoplatform for various biomedical applications. |
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language | English |
last_indexed | 2024-03-10T08:59:32Z |
publishDate | 2021-07-01 |
publisher | MDPI AG |
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spelling | doaj.art-81d84a782a0c4d41a5563524ac076efa2023-11-22T06:51:07ZengMDPI AGBiomedicines2227-90592021-07-019885810.3390/biomedicines9080858Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible NanoplatformAtanu Naskar0Sohee Lee1Dongjoon Ko2Semi Kim3Kwang-sun Kim4Department of Chemistry and Chemistry, Institute for Functional Materials, Pusan National University, Busan 46241, KoreaDepartment of Chemistry and Chemistry, Institute for Functional Materials, Pusan National University, Busan 46241, KoreaImmunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, KoreaImmunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, KoreaDepartment of Chemistry and Chemistry, Institute for Functional Materials, Pusan National University, Busan 46241, KoreaThe interactions between proteins and nanoparticles need to be fully characterized as the immobilization of proteins onto various nanoplatforms in the physiological system often results in the change of surface of the protein molecules to avoid any detrimental issues related to their biomedical applications. Hence, in this article, the successful low-temperature synthesis of a BP-based γ-Fe<sub>2</sub>O<sub>3</sub> (IB) nanocomposite and its interactive behavior with bovine serum albumin (BSA)—a molecule with chemical similarity and high sequence identity to human serum albumin—are described. To confirm the formation of γ-Fe<sub>2</sub>O<sub>3</sub> and the IB nanocomposite, X-ray diffraction, transmission electron microscopy, and X-ray photoelectron spectroscopy analyses of the materials were performed. Additionally, the physical interaction between BSA and the IB nanocomposite was confirmed via UV–Vis and photoluminescence spectral analyses. Finally, the biocompatibility of the BSA-immobilized IB nanocomposite was verified using an in vitro cytotoxicity assay with HCT-15 colon cancer cells. Our findings demonstrate that this newly developed nanocomposite has potential utility as a biocompatible nanoplatform for various biomedical applications.https://www.mdpi.com/2227-9059/9/8/858black phosphorus nanocompositenanomaterial–protein interactionserum albumin proteiniron oxide nanocompositenanoplatform |
spellingShingle | Atanu Naskar Sohee Lee Dongjoon Ko Semi Kim Kwang-sun Kim Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform Biomedicines black phosphorus nanocomposite nanomaterial–protein interaction serum albumin protein iron oxide nanocomposite nanoplatform |
title | Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform |
title_full | Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform |
title_fullStr | Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform |
title_full_unstemmed | Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform |
title_short | Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe<sub>2</sub>O<sub>3</sub> Nanocomposites: A Promising Biocompatible Nanoplatform |
title_sort | bovine serum albumin immobilized black phosphorus based γ fe sub 2 sub o sub 3 sub nanocomposites a promising biocompatible nanoplatform |
topic | black phosphorus nanocomposite nanomaterial–protein interaction serum albumin protein iron oxide nanocomposite nanoplatform |
url | https://www.mdpi.com/2227-9059/9/8/858 |
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