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Probing Bio-Nano Interactions between Blood Proteins and Monolayer-Stabilized Graphene Sheets

  Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimesional (2D) material for nanomedecine, but its... Full description

Journal Title: Small Nov 2015, Vol.11(43), pp.5814-5825
Main Author: Gan, Shiyu
Other Authors: Zhong, Lijie , Han, Dongxue , Niu, Li , Chi, Qijin
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 16136810 ; E-ISSN: 16136829 ; DOI: 10.1002/smll.201501819
Link: http://search.proquest.com/docview/1757685337/?pq-origsite=primo
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title: Probing Bio-Nano Interactions between Blood Proteins and Monolayer-Stabilized Graphene Sheets
format: Article
creator:
  • Gan, Shiyu
  • Zhong, Lijie
  • Han, Dongxue
  • Niu, Li
  • Chi, Qijin
subjects:
  • Proteins
ispartof: Small, Nov 2015, Vol.11(43), pp.5814-5825
description:   Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimesional (2D) material for nanomedecine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long-term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, [gamma]-globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main drving forces for blood protein binding involve the π-π interacations between the π-plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
language: eng
source:
identifier: ISSN: 16136810 ; E-ISSN: 16136829 ; DOI: 10.1002/smll.201501819
fulltext: fulltext
issn:
  • 16136810
  • 1613-6810
  • 16136829
  • 1613-6829
url: Link


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description  Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimesional (2D) material for nanomedecine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long-term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, [gamma]-globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main drving forces for blood protein binding involve the π-π interacations between the π-plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
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description  Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimesional (2D) material for nanomedecine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long-term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, [gamma]-globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main drving forces for blood protein binding involve the π-π interacations between the π-plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
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abstract  Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimesional (2D) material for nanomedecine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long-term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, [gamma]-globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main drving forces for blood protein binding involve the π-π interacations between the π-plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
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doi10.1002/smll.201501819
urlhttp://search.proquest.com/docview/1757685337/
date2015-11-01