J. Mater. Sci. Technol. ›› 2020, Vol. 46: 74-87.DOI: 10.1016/j.jmst.2020.01.008
• Invited Review • Previous Articles Next Articles
Xing Zhoua,b,c, Jian Sub, Chenxi Wanga, Changqing Fanga,c,**(), Xinyu Hea, Wanqing Leia,c, Chaoqun Zhangd, Zhigang Huange,*()
Received:
2019-03-15
Revised:
2019-09-22
Accepted:
2019-09-23
Published:
2020-06-01
Online:
2020-06-19
Contact:
Changqing Fang,Zhigang Huang
About author:
Xing Zhou is currently an associate Professor at the Xi’an University of Technology, China. His research is focused on waterborne polyurethane synthesis and the application in water-based printing ink and packaging adhesion, recycling of waste packaging polymers, and nanohybrids. So far, he has published more than 30 papers in international peer-reviewed journals.|Changqing Fang is currently a Professor at the Xi’an University of Technology, China. He is the dean of ‘Faculty of Printing, Packaging Engineering and Digital Media Technology’. His research is focused on the recycling of waste packaging plastic and the preparation of novel packaging materials. So far, he has published nearly 120 papers in international peer-reviewed journals. The papers have been cited more than 1000 times.|Zhigang Huang is a Professor at the Beijing Technology and Business University, China. His research is focused on process control of packaging materials and the application in food. He is currently a senior researcher and group leader of the School of Material and Mechanical Engineering.
Xing Zhou, Jian Su, Chenxi Wang, Changqing Fang, Xinyu He, Wanqing Lei, Chaoqun Zhang, Zhigang Huang. Design, preparation and measurement of protein/CNTs hybrids: A concise review[J]. J. Mater. Sci. Technol., 2020, 46: 74-87.
Peptide and Protein | CNTs | The index of CNTs | Reason for their interactions | Method | Refs. |
---|---|---|---|---|---|
Ferritin and streptavidin | SWCNTs | Diameter ~10 nm | Immobilization of protein | Noncovalent functionalizati of CNTs sidewalls | [ |
De novo peptides (such as amphiphilic α-helical peptide) | SWCNTs | Diameter 0.7-1.4 nm | Dispersion of CNTs | Sonication | [ |
De novo peptides | SWCNTs | / | Immunization with Biofunctionalized CNTs | Stirring and deposition | [ |
Oligoglycine peptides (tectomers) | MWCNTs/SWCNTs | Diameter 20-40 nm/Average diameter 1 nm; Length 1 μm | Functional hybrids | Sonication | [ |
Cyclic peptide | MWCNTs | / | Sorting CNTs | Incubation | [ |
Phage-displayed peptides | MWCNTs | Diameter2?10 nm | Targeted Carriers for Therapeutic and Imaging Materials | Phage-displayed technique | [ |
Myoglobin | MWCNTs | Diameter 10-15 nm (outer), 2-6 nm (inner); Lengths 0.1-10 μm | detection of cardiac myoglobin | Sequential drop casting | [ |
Human cellular proteins | MWCNTs | Diameter 20-40 nm | Selection of proteins | Incubation | [ |
Bovine serum albumin | MWCNTs | Diameter <10 nm, 10-20 nm and 20-40 nm | Interaction mechanism | Incubation | [ |
Albumin | SWCNTs | Diameter0.7-1.4 nm | Functional hybrids | Sonication | [ |
Nuclear protein | SWCNTs | Diameter 1.0 ± 0.3 nm; Length 145 ± 17 nm | Targeted Carriers for Therapeutic and Imaging Materials | Sonication | [ |
Kinesin-1 motor proteins | SWCNTs | Diameter~1 nm; Length>10 μm | New intermediate mode | Sonication | [ |
Arabinogalactan protein | SWCNTs | Diameter <2 nm (outer); Length 5-30 μm | Dispersion of CNTs | Sonication | [ |
Lysozyme | SWCNTs | / | Dispersion of CNTs | Sonication | [ |
α-chymotrypsin | MWCNTs | Diameter 10-20 nm | CNT Alteration of Protein Functioning | Incubation | [ |
Horseradish peroxidase | SWCNTs | / | Biodegradation of SWCNTs | Incubation | [ |
Laccase | MWCNTs | Diameter10-20 nm; Length 5-15 μm | Immobilization of protein | Orbital stirring and washing | [ |
Human immune protein | MWCNTs | Diameter ~25 nm | Disaggregation of CNTs | Sonication | [ |
Table 1 Information of peptide and proteins interacting with carbon nanotubes.
Peptide and Protein | CNTs | The index of CNTs | Reason for their interactions | Method | Refs. |
---|---|---|---|---|---|
Ferritin and streptavidin | SWCNTs | Diameter ~10 nm | Immobilization of protein | Noncovalent functionalizati of CNTs sidewalls | [ |
De novo peptides (such as amphiphilic α-helical peptide) | SWCNTs | Diameter 0.7-1.4 nm | Dispersion of CNTs | Sonication | [ |
De novo peptides | SWCNTs | / | Immunization with Biofunctionalized CNTs | Stirring and deposition | [ |
Oligoglycine peptides (tectomers) | MWCNTs/SWCNTs | Diameter 20-40 nm/Average diameter 1 nm; Length 1 μm | Functional hybrids | Sonication | [ |
Cyclic peptide | MWCNTs | / | Sorting CNTs | Incubation | [ |
Phage-displayed peptides | MWCNTs | Diameter2?10 nm | Targeted Carriers for Therapeutic and Imaging Materials | Phage-displayed technique | [ |
Myoglobin | MWCNTs | Diameter 10-15 nm (outer), 2-6 nm (inner); Lengths 0.1-10 μm | detection of cardiac myoglobin | Sequential drop casting | [ |
Human cellular proteins | MWCNTs | Diameter 20-40 nm | Selection of proteins | Incubation | [ |
Bovine serum albumin | MWCNTs | Diameter <10 nm, 10-20 nm and 20-40 nm | Interaction mechanism | Incubation | [ |
Albumin | SWCNTs | Diameter0.7-1.4 nm | Functional hybrids | Sonication | [ |
Nuclear protein | SWCNTs | Diameter 1.0 ± 0.3 nm; Length 145 ± 17 nm | Targeted Carriers for Therapeutic and Imaging Materials | Sonication | [ |
Kinesin-1 motor proteins | SWCNTs | Diameter~1 nm; Length>10 μm | New intermediate mode | Sonication | [ |
Arabinogalactan protein | SWCNTs | Diameter <2 nm (outer); Length 5-30 μm | Dispersion of CNTs | Sonication | [ |
Lysozyme | SWCNTs | / | Dispersion of CNTs | Sonication | [ |
α-chymotrypsin | MWCNTs | Diameter 10-20 nm | CNT Alteration of Protein Functioning | Incubation | [ |
Horseradish peroxidase | SWCNTs | / | Biodegradation of SWCNTs | Incubation | [ |
Laccase | MWCNTs | Diameter10-20 nm; Length 5-15 μm | Immobilization of protein | Orbital stirring and washing | [ |
Human immune protein | MWCNTs | Diameter ~25 nm | Disaggregation of CNTs | Sonication | [ |
Fig. 1. The adsorption mode between CNTs and a monoclonal antibody (mAb). (a) graphical representation of CNT-Ab complex with the CNTs diameter of 20 ?; (b) graphical representation of CNT-Ab complex with the CNTs diameter of 80 ?; (c) the function of the CNTs diameter docked onto the equilibrated structure of mAb [30]. Copyright 2013, Wiley.
Fig. 2. Combination self-assembly between the peptide and the CNTs can lead to the stabilization of the α-helix (the processes in red block depict the peptide chameleon depending on the different types of CNTs) [31]. Copyright 2013, ACS.
Fig. 5. The folding and non-folding of proteins (a) Involvement of intrinsic disorder in protein function [37]; (b) Comparison of a naturally directed polypeptideand an oppositely directed polypeptide [38]. Copyright 2014, ACS.
Fig. 6. The 3D structures of the 20 proteinogenic amino acids (AA) are reported and classified according to the nature of the side chains: hydrophobic, sulfur-containing, aromatic, charged, polar and cyclic. For each AA, the common nomenclature, the full name, the three letters and the one-letter abbreviations are reported [15], and the lone pair electrons (Lp in the 3D structures) are presented. Copyright 2015, RSC.
Fig. 7. Cartoon of the conjugated between CNTs and proteins with different dimensional structures. (a) The influence of amino acid [1] Copyright 2013, ACS; (b) The influence of secondary structure [22] Copyright 2014, Wiley; (c) The function of tertiary structure [11]; (d) The function of quaternary structure [11]. Copyright 2011, AAAS.
Fig. 8. The functional of secondary or tertiary structure binding to CNTs surface. (a) The multivalent ligand switching phenomenon under photothermal control for peptide/CNTs hybrid; (b) Schematic diagram of MWCNT-COOH/2 T tectomer interaction. COO- groups in CNT provides useful anchor sites for tectomers, the electrostatic forces between NH-3 and COO- groups being the driving force of hybrid formation [35] Copyright 2017, RSC; (c) Schematic diagram for the binding of the modified CNTs with α-ChT [24] Copyright 2015, ACS; (d) space-filling models of BSA/CNT hybrid to indicate protein electrostatic surface potential at different degrees of rotation and the potential binding site [32]. Copyright 2015, Elsevier.
Fig. 9. Different types of measurements that provide information on the forces between particles and surfaces. (a) Adhesion measurements (practical applications: xerography, particle adhesion, powder technology, ceramicprocessing). (b) Peeling measurements (practical applications: adhesive tapes, material fracture and crack propagation). (c) Direct measurements of force as a function of surface separation (practical applications: testing theories of inter-surface forces). (d) Contact angle measurements (practical applications: testing wettability and stability of surface films, detergency). (e) Equilibrium thickness of thin free films (practical applications: soap films, foams). (f) Equilibrium thickness of thin adsorbed films (practical applications: wetting of hydrophilic surfaces by water, adsorption of molecules from vapor, various magnetic and opto-electronic films, protective coatings and lubricant layers, biosensors). (g) Interparticle spacing in liquids using various spectroscopic and scattering techniques (practical applications: colloidal dispersions, paints, pharmaceutical dispersions, nano- and micro-structured composite materials, measuring intermacromolecular and interparticle forces). (h) Sheet-like particle spacings in liquids (practical applications: clay and soil swelling behavior, microstructure of soaps and biological membranes, composite materials). (i) Coagulation studies (practical application: basic experimental technique for testing the stability and coagulationrates of colloidal dispersions) [59]. Copyright 2011, Elsevier.
Fig. 10. Scheme of the SFA and AFM functions in measuring the interactions. (a) The schematic setup of the friction experiments of aqueous HA-coated CNT dispersions. The CNTs were confined between two smooth surfaces at a separation distance D in a sphere-on-flat surfaces with radius of curvature R =2 cm. The main interactions in the system are the CNT-surface and CNT-CNT interactions. At high compressive pressure of the surfaces (normal force, F⊥, pressure P = F⊥/π r2) the contact area π r2 flattens due to elasticity of the glue layer. Typical dimensions of the CNTs are l =1 μm length, φ = 2 nm for SWCNTs and φ = 25 ± 10 nm for MWCNTs. The CNTs have a layer of HA that behaves as polymeric surfactant and, in pure water, is believed to extend several nm into the solution [65] Copyright 2011, Wiley; (b) Schematic of the AFM probe functionalization with graphene oxide. Procedure (a): Immersion of the AFM cantilever in an aqueous solution of dopamine results in deposition of a thin adherent film of polydopamine on the probe surface; Procedure (b): Subsequent immersion in an aqueous dispersion of graphene oxide results in immobilization of the nanomaterial on the probe surface. The components of the functionalized probe surface are depicted in procedure (c), where polydopamine is described as a supramolecular aggregate of dopamine monomers [66] Copyright 2016, ACS; (c) Applying AFM to probe interaction forces (F) of single biomolecules [64]. Copyright 2008, Springer.
Fig. 12. Cartoon of CNTs/proteins hybrid and their applications in different fields. (a, b) The conjugated of CNTs and proteins [30], Copyright 2013, Wiley; (c) Fibronectin-CNTs hybrid nanostructures to control the adhesion and growth of cells [85]; Copyright 2011, Wiley; (d) The single lysozyme molecule to a carbon nanotube to produce stable FET with high-bandwidth transducer for protein motion [86], Copyright 2012, AAAS; (e) The detection of biotin-streptavidin binding by changes in device characteristics [87], Copyright 2003, ACS; (f) Cartoon of the CNTs passing cellular membranes [79], Copyright 2010, Springer; (g) Diagrams of screening printing and pen directly writing of the CNTs/lysozyme hybrids [84].
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