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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 st... Full description

Journal Title: Small November 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
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ID: ISSN: 1613-6810 ; E-ISSN: 1613-6829 ; DOI: 10.1002/smll.201501819
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recordid: wj10.1002/smll.201501819
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:
  • Blood Proteins
  • Chemically Converted Graphene
  • Graphene Nanochemistry
  • Nanomedicine
  • Perylene
ispartof: Small, November 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, γ‐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. and monolayer‐stabilized graphene nanosheets in pseudo‐physiological buffer solutions is studied to reveal key control factors.
language:
source:
identifier: ISSN: 1613-6810 ; E-ISSN: 1613-6829 ; DOI: 10.1002/smll.201501819
fulltext: fulltext
issn:
  • 1613-6810
  • 16136810
  • 1613-6829
  • 16136829
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titleProbing Bio–Nano Interactions between Blood Proteins and Monolayer‐Stabilized Graphene Sheets
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subjectBlood Proteins ; Chemically Converted Graphene ; Graphene Nanochemistry ; Nanomedicine ; Perylene
descriptionMeeting 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, γ‐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. and monolayer‐stabilized graphene nanosheets in pseudo‐physiological buffer solutions is studied to reveal key control factors.
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descriptionMeeting 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, γ‐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. and monolayer‐stabilized graphene nanosheets in pseudo‐physiological buffer solutions is studied to reveal key control factors.
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abstractMeeting 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, γ‐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. and monolayer‐stabilized graphene nanosheets in pseudo‐physiological buffer solutions is studied to reveal key control factors.
doi10.1002/smll.201501819
pages5814-25
date2015-11