The Role of the Protein Corona in Fiber Structure-Activity Relationships
Abstract
:1. Introduction
Human Exposure to (Nano)fibers
2. Methods to Determine the Protein Coating of (Nano)materials
3. Interactions of Proteins and Fibers
3.1. Asbestos-Protein Interactions
Year of publication | Type of study | Type of adsorbed protein(s) | Major outcome | Reference |
---|---|---|---|---|
1974 | Protein adsorption | Human serum albumin | The surface charge of the asbestos fibers had a strong influence on the adsorption of proteins. | [31] |
1977 | In vitro, in vivo | Human serum albumin | The capacity of asbestos fibers to adsorb proteins is dependent from the magnesium content in the fibers. | [33] |
1980 | Protein adsorption | Bovine serum albumin, Ferritin | Magnesium depletion of the asbestos fibers leads to a decrease of albumin adsorption, while the specific adsorption offerritin increased. | [34] |
1986 | Protein adsorption | Fetal serum proteins | Strong electrostatic interactions between the charges of the fibers and the proteins were responsible for the protein-fiber adsorption. | [35] |
1987 | Protein adsorption | Different types of proteins | The protein-fiber affinity was correlated with the specific area of the fiber and the protein charge density. | [36] |
1990 | In vitro | Serum proteins | The cytotoxic effects of asbestos fibers was serum-dose dependent. | [37] |
Immunoglobulin G, Bovine serum albumin, Cytochrome c | Certain proteins were selectively adsorbed onto the asbestos fibers. | [38] | ||
1995 | In vitro | Vitronectin, Fibronectin | Vitronectin specifically enhanced the internalization of asbestos fibers via αvβ5 integrin receptors. | [39] |
2000 | In vitro | Vitronectin | The adsorption of vitronectin onto the asbestos fibers increased the fiber uptake and the cytotoxic effects of asbestos. | [40] |
Vitronectin adsorption to chrysotile asbestos fibers increased fiber phagocytosis and toxicity for mesothelial cells. | [41] |
3.2. CNT-Protein Interactions
3.2.1. Mechanism of Interaction
3.2.2. Influence of Solvents, Surfactants, Surface-Functionalization, and Pre-Coating on CNT-Protein Interactions
3.2.3. Alternative Theory to CNT Protein Interactions
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- Electrochemical and chemical nature of the CNT and proteins are essential for strong CNT-protein interaction
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- Protein-CNT binding is based on non-covalent π-π stacking hydrophobic interactions
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- The diameter, size and surface curvature of the CNT is essential for a significant protein-CNT binding
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- Protein-binding is dependent on the three-dimensional arrangement of the carbon atoms of the CNTs
Year of publication | Type of CNT | Type of adsorbed protein(s) | Major outcome | Reference |
---|---|---|---|---|
2001 | SWCNT | Ferritin, streptavidin | Proteins with primary and secondary amines adsorbed onto f-SWCNT via π-π stacking interactions. | [82] |
Proteins rich in surface amines (antibody for C60) | SWCNT with a curved hydrophobic π-electron-rich surface bound on the hydrophobic binding sites of proteins. | [54] | ||
2002 | SWCNT | Metalloproteins, Enzymes | Enzymes immobilized on SWCNTs retain their catalytic activity. | [68] |
Streptavidin (various proteins) | Pre-coating of SWCNTs with triton X-100 prior PEG coating prevented the adsorption of small proteins onto SWCNT nearly completely. | [78] | ||
2003 | SWCNT | Amphiphilic α-helical peptide | The apolar residues of amphiphilic proteins bound to the surface of SWCNT and the polar residues of the proteins were located against the solvent face. | [55] |
MWCNT | Phage and other types of peptides | Peptides that were rich in histidine and tryptophan bound at special locations of the MWCNTs by hydrophobic interactions. | [62] | |
2004 | SWCNT | α-Chymotrypsin, soybean peroxidase | The enzymes changed their secondary structures upon adsorption onto the SWCNTs, which caused a decrease or nearly complete loss of their activity. | [66] |
Ferritin | A covalent coating of SWCNT with PEG was alleviating or even completely eliminating the natural protein affinity of the SWCNTs. | [77] | ||
Amphiphilic α-helical peptide | The binding of polar residues of amphiphilic proteins onto the surface of SWCNTs increased the dispersion of the SWCNTs in water. | [56] | ||
CNT | Streptavidin | Protein adsorption onto CNTs occurred through interactions between the amine groups of the protein and the hydrophobic surface of the CNTs. | [83] | |
2005 | SWCNT | Amphiphilic α-helical peptide | Amphiphilic peptides bound non-covalently with their apolar residues onto the SWCNTs, which resulted in a better solubilisation of the SWCNTs. | [51] |
Amphiphilic peptide helix (nano-1) | The aromatic residues of the peptides interacted with the SWCNT surface, which was leading to a better dispersion of the SWCNTs. | [52] | ||
2006 | SWCNT | Model proteins | Protein coated SWCNTs were incorporated by the cells via energy dependent endocytosis through clathrin-coated pits. | [84] |
Different types of proteins | Proteins adsorbed onto SWCNTs via π-π stacking as well as amine interactions, whereas the hydrophilic protein moieties were located towards the water face. | [57] | ||
Polyline, polytryptophan | A strong adhesive force was registrated between the protonated amine-groups of the protein (polylysine) and the carboxyl-groups of the oxidized CNTs. | [58] | ||
Lysozyme | π-π stacking and hydrophobic interactions as well as protonated amine interactions between proteins and SWCNT were responsible for the dispersion of the SWCNTs. | [49] | ||
Fibrinogen, apolipoproteins (AI, AIV, CIII) | Protein binding onto SWCNT was highly selective. | [45] | ||
Peptides from phage libraries | Hydrophobic as well as π-π interactions between proteins and SWCNTs were important for a selective protein binding onto SWCNTs. | [46] | ||
2007 | SWCNT | Foetal bovine plasma, human serum/plasma protein | The uptake of SWCNT occurred by pathways associated with the adsorbed proteins. The proteins modulated in addition the toxicity of the SWCNTs. | [43] |
Different types of proteins | The primary, secondary and tertiary structures of proteins and the pH of the dispersion medium were important to obtain a high yield of de-bundeled CNTs | [61]. | ||
Different types of peptides | Disulfide bonds adsorbed onto the SWCNTs and by that they solubilize the SWCNTs without altering their electronic structure. | [60] | ||
DWCNT | Surfactant proteins A and D | Supernatant protein A and D adsorbed selectively onto DWCNTs out of different pulmonary surfactant protein samples. | [59] | |
2008 | SWCNT, MWCNT | Ribonuclease A | CNTs functionalized with carboxylic groups interacted with the enzyme and caused a reduction of its activity by changing its conformation. | [64] |
MWCNT, f-MWCNT | Bovine serum albumin (BSA) and different types of proteins | Electrostatic and stereo-chemical properties of the MWCNTs and the proteins as well as the curvature of the MWCNTs were affecting the protein binding affinity onto the MWCNTs. | [81] | |
Human plasma and serum proteins | Functionalization of the MWCNTs affected the patterns of adsorbed proteins onto the MWCNT, which resulted in a better biocompatibility of the MWCNTs. | [76] | ||
CNT | A-sub-domain of human serum albumin | The adsorption of proteins onto CNTs caused a conformation change of the secondary protein structure, which resulted in a decrease of the protein activity. | [67] | |
2009 | MWCNT, f-MWCNT | α-Chymotrypsin | Enzymes bound onto MWCNTs through π-π stacking and hydrophobic interactions, which resulted in a competitive inhibition of the enzyme activity. | [65] |
2010 | SWCNT | Model surfactant | Surfactants with a larger hydrophilic head group was leading to a significant better dispersion stability of SWCNTs. | [75] |
Model protein | Hydrophobic interactions between the hydrophobic core of the proteins and the SWCNTs formed stable complexes, which caused a blockage of the active sides of the proteins. | [63] | ||
MWCNT, f-MWCNT | Pulmonary surfactant (Curosurf®) | The pre-coating of MWCNTs with a lung surfactant influenced the protein binding onto the MWCNTs and resulted in characteristic binding patterns. | [70] | |
2011 | SWCNT, MWCNT | Serum proteins | The adsorption capacity of CNTs for proteins was dependent on the type, arrangement model, size and surface modification of the CNTs. | [42] |
SWCNT | Human serum proteins | Competitive binding of blood proteins onto the SWCNT surface can alter the cellular interaction pathways, resulting in a reduced cytotoxicity. | [44] | |
2011 | SWCNT | Bovine serum albumin (BSA) | Bovine serum albumin dispersed SWCNTs readily entered into the cells and did not acute deleterious cellular effects. | [73] |
SWCNT, DWCNT | Serum proteins | The adsorption of enzymes of the immune system to the hydrophobic SWCNT surface didn’t caused an activation of the enzymes. | [85] | |
MWCNT | Blood proteins | A surface modification of the MWCNT affected their patterns of adsorbed proteins, which resulted in a modification of the biocompatibility of the MWCNTs. | [48] | |
2012 | SWCNT | Bovine serum albumin (BSA) | Bovine serum albumin coated SWCNTs were taken up by the cells within seconds. However, the cells were able to expel the incorporated BSA-SWCNT complexes over hours and days. | [72] |
Different types of proteins | The stability of a SWCNT-protein complex had a substantial influence on the cellular uptake and the uptake of a certain protein was dependent from the cell type. | [86] | ||
MWCNT | Pulmonary surfactant (Curosurf) | The pre-coating of MWCNTs with a lung surfactant affected the uptake of the MWCNTs without significantly altering the cytotoxicity of the MWCNTs. | [71] | |
2013 | MWCNT | Human cellular proteins (HeLa cells lysate) | Electrostatic, stereochemical properties, diameter and curvature of the MWCNTs were significantly affecting the adsorption of proteins onto the MWCNTs. | [79] |
SWCNT | Plasma proteins | The surface PEG conformation of SWCNT-PEG complexes affected the pattern of adsorbed plasma proteins onto the SWCNTs and influenced the biodistribution of the SWCNT-PEG complexes. | [53] | |
SWCNT, f-SWCNT, MWCNT, f-MWCNT | Foetal Bovine serum (FBS) | Functionalized CNTs were able to bind a number of unique proteins, which implied that electrostatic interactions and specific covalent bonding were involved. | [80] | |
CNT | Different types of proteins | π-π stacking and hydrophobic interactions were responsible for the adsorption of proteins onto CNTs. The protein adsorption leaded to a reduction of the cytotoxicity and to a loss of the enzymatic activity of the proteins. | [47] |
4. Discussion
4.1. Comparison of Protein Coronas
4.2. Methodology and Challenges
4.3. Influence of Shape on Nanomaterial-Protein Interaction
Acknowledgments
Author Contributions
Conflicts of Interest
References
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Kucki, M.; Kaiser, J.-P.; Clift, M.J.D.; Rothen-Rutishauser, B.; Petri-Fink, A.; Wick, P. The Role of the Protein Corona in Fiber Structure-Activity Relationships. Fibers 2014, 2, 187-210. https://doi.org/10.3390/fib2030187
Kucki M, Kaiser J-P, Clift MJD, Rothen-Rutishauser B, Petri-Fink A, Wick P. The Role of the Protein Corona in Fiber Structure-Activity Relationships. Fibers. 2014; 2(3):187-210. https://doi.org/10.3390/fib2030187
Chicago/Turabian StyleKucki, Melanie, Jean-Pierre Kaiser, Martin J. D. Clift, Barbara Rothen-Rutishauser, Alke Petri-Fink, and Peter Wick. 2014. "The Role of the Protein Corona in Fiber Structure-Activity Relationships" Fibers 2, no. 3: 187-210. https://doi.org/10.3390/fib2030187
APA StyleKucki, M., Kaiser, J. -P., Clift, M. J. D., Rothen-Rutishauser, B., Petri-Fink, A., & Wick, P. (2014). The Role of the Protein Corona in Fiber Structure-Activity Relationships. Fibers, 2(3), 187-210. https://doi.org/10.3390/fib2030187