Advancing Albumin Isolation from Human Serum with\nGraphene Oxide and Derivatives: A Novel Approach for Clinical Applications

This study introduces\na novel, environmentally friendly albumin\nisolation method using graphene oxide (GO). GO selectively extracts\nalbumin from serum samples, leveraging the unique interactions between\nGO’s oxygen-containing functional groups and serum proteins.\nThis method achieves high purification efficiency without the need\nfor hazardous chemicals. Comprehensive characterization of GO and\nreduced graphene oxide (rGO) through techniques such as X-ray diffraction\n(XRD) analysis, Raman spectroscopy, scanning electron microscopy (SEM),\nand Fourier transform infrared spectroscopy (FTIR) confirmed the structural\nand functional group transformations crucial for protein binding.\nSodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE)\nand mass spectrometry analyses demonstrated over 95% purity of isolated\nalbumin, with minimal contamination from other serum proteins. The\ndeveloped method, optimized for pH and incubation conditions, showcases\na green, cost-effective, and simple alternative for albumin purification,\npromising broad applicability in biomedical research and clinical\napplications.

Publication Details

Journal
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Published
2024-09-20
DOI
https://doi.org/10.1021/acsomega.4c04276.s001
Primary Topic
Plant Taxonomy and Phylogenetics
Type
article
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article

Advancing Albumin Isolation from Human Serum with\nGraphene Oxide and Derivatives: A Novel Approach for Clinical Applications

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Plant Taxonomy and Phylogenetics
article

Advancing Albumin Isolation from Human Serum with\nGraphene Oxide and Derivatives: A Novel Approach for Clinical Applications

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Abstract

This study introduces\na novel, environmentally friendly albumin\nisolation method using graphene oxide (GO). GO selectively extracts\nalbumin from serum samples, leveraging the unique interactions between\nGO’s oxygen-containing functional groups and serum proteins.\nThis method achieves high purification efficiency without the need\nfor hazardous chemicals. Comprehensive characterization of GO and\nreduced graphene oxide (rGO) through techniques such as X-ray diffraction\n(XRD) analysis, Raman spectroscopy, scanning electron microscopy (SEM),\nand Fourier transform infrared spectroscopy (FTIR) confirmed the structural\nand functional group transformations crucial for protein binding.\nSodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE)\nand mass spectrometry analyses demonstrated over 95% purity of isolated\nalbumin, with minimal contamination from other serum proteins. The\ndeveloped method, optimized for pH and incubation conditions, showcases\na green, cost-effective, and simple alternative for albumin purification,\npromising broad applicability in biomedical research and clinical\napplications.

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Plant Taxonomy and Phylogenetics
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