Adsorption of Bovine Serum Albumin on Carbon-Based Materials

The protein adsorption plays a very important role in biotechnology, biomolecular engineering and it is one of the main factors determining bio- and hemocompatibility of biomedical materials in medical applications, such as blood purification and wound healing. Here we report adsorption properties o...

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Main Authors: Mykola Seredych, Lyuba Mikhalovska, Sergey Mikhalovsky, Yury Gogotsi
Format: Article
Language:English
Published: MDPI AG 2018-01-01
Series:C
Subjects:
Online Access:http://www.mdpi.com/2311-5629/4/1/3
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author Mykola Seredych
Lyuba Mikhalovska
Sergey Mikhalovsky
Yury Gogotsi
author_facet Mykola Seredych
Lyuba Mikhalovska
Sergey Mikhalovsky
Yury Gogotsi
author_sort Mykola Seredych
collection DOAJ
description The protein adsorption plays a very important role in biotechnology, biomolecular engineering and it is one of the main factors determining bio- and hemocompatibility of biomedical materials in medical applications, such as blood purification and wound healing. Here we report adsorption properties of two carbon-based materials, thermally expanded graphite (EGr) and graphene nanoplatelets (GnP), for bovine serum albumin (BSA), the most abundant blood plasma protein. The influence of the surface chemistry of expanded graphite on the mechanism of BSA adsorption was studied by using EGr modified with oxygen or nitrogen functionalities. Having low microporosity and the specific surface area in the range of 5 to 50 m2/g, the expanded graphite exhibits high protein adsorption capacity at high equilibrium concentrations, which makes this material a potential candidate for biomedical applications as a carrier for high molecular weight (HMW) drug delivery or adsorption of HMW metabolites. At low equilibrium concentrations, the effect of specific protein-surface functional groups interaction reveals the differences between the adsorption affinity of different surface modified EGr materials to BSA. The adsorption of BSA on GnP with a specific surface area of 286 m2/g and a developed micro-/mesoporous structure did not follow the same mechanism as seen with EGr materials. At low equilibrium concentration of BSA, GnP exhibits high adsorption efficiency. An important finding is that no release of nanoparticles from expanded graphite adsorbents was observed, which makes them potentially suitable for direct contact with blood and other tissues while very small nanoparticles were noticed in the case of graphene nanoplatelets.
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spelling doaj.art-e2817ec7a4fe47cc9018895554c878d32022-12-21T19:44:13ZengMDPI AGC2311-56292018-01-0141310.3390/c4010003c4010003Adsorption of Bovine Serum Albumin on Carbon-Based MaterialsMykola Seredych0Lyuba Mikhalovska1Sergey Mikhalovsky2Yury Gogotsi3Department of Materials Science & Engineering and A.J. Drexel Nanomaterials Institute, Drexel University, Philadelphia, PA 19104, USASchool of Pharmacy and Biomolecular Sciences, University of Brighton, Brighton BN2 4GJ, UKSchool of Pharmacy and Biomolecular Sciences, University of Brighton, Brighton BN2 4GJ, UKDepartment of Materials Science & Engineering and A.J. Drexel Nanomaterials Institute, Drexel University, Philadelphia, PA 19104, USAThe protein adsorption plays a very important role in biotechnology, biomolecular engineering and it is one of the main factors determining bio- and hemocompatibility of biomedical materials in medical applications, such as blood purification and wound healing. Here we report adsorption properties of two carbon-based materials, thermally expanded graphite (EGr) and graphene nanoplatelets (GnP), for bovine serum albumin (BSA), the most abundant blood plasma protein. The influence of the surface chemistry of expanded graphite on the mechanism of BSA adsorption was studied by using EGr modified with oxygen or nitrogen functionalities. Having low microporosity and the specific surface area in the range of 5 to 50 m2/g, the expanded graphite exhibits high protein adsorption capacity at high equilibrium concentrations, which makes this material a potential candidate for biomedical applications as a carrier for high molecular weight (HMW) drug delivery or adsorption of HMW metabolites. At low equilibrium concentrations, the effect of specific protein-surface functional groups interaction reveals the differences between the adsorption affinity of different surface modified EGr materials to BSA. The adsorption of BSA on GnP with a specific surface area of 286 m2/g and a developed micro-/mesoporous structure did not follow the same mechanism as seen with EGr materials. At low equilibrium concentration of BSA, GnP exhibits high adsorption efficiency. An important finding is that no release of nanoparticles from expanded graphite adsorbents was observed, which makes them potentially suitable for direct contact with blood and other tissues while very small nanoparticles were noticed in the case of graphene nanoplatelets.http://www.mdpi.com/2311-5629/4/1/3bovine serum albuminexpanded graphitegraphene nanoplateletsadsorption
spellingShingle Mykola Seredych
Lyuba Mikhalovska
Sergey Mikhalovsky
Yury Gogotsi
Adsorption of Bovine Serum Albumin on Carbon-Based Materials
C
bovine serum albumin
expanded graphite
graphene nanoplatelets
adsorption
title Adsorption of Bovine Serum Albumin on Carbon-Based Materials
title_full Adsorption of Bovine Serum Albumin on Carbon-Based Materials
title_fullStr Adsorption of Bovine Serum Albumin on Carbon-Based Materials
title_full_unstemmed Adsorption of Bovine Serum Albumin on Carbon-Based Materials
title_short Adsorption of Bovine Serum Albumin on Carbon-Based Materials
title_sort adsorption of bovine serum albumin on carbon based materials
topic bovine serum albumin
expanded graphite
graphene nanoplatelets
adsorption
url http://www.mdpi.com/2311-5629/4/1/3
work_keys_str_mv AT mykolaseredych adsorptionofbovineserumalbuminoncarbonbasedmaterials
AT lyubamikhalovska adsorptionofbovineserumalbuminoncarbonbasedmaterials
AT sergeymikhalovsky adsorptionofbovineserumalbuminoncarbonbasedmaterials
AT yurygogotsi adsorptionofbovineserumalbuminoncarbonbasedmaterials