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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Main Authors: Atanu Naskar, Sohee Lee, Dongjoon Ko, Semi Kim, Kwang-sun Kim
Format: Article
Language:English
Published: MDPI AG 2021-07-01
Series:Biomedicines
Subjects:
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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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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