Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Influence of carbon nanomaterial defects on the formation of protein corona.

ABSTRACT: In any physiological media, carbon nanomaterials (CNM) strongly interact with biomolecules leading to the formation of biocorona, which subsequently dictate the physiological response and the fate of CNMs. Defects in CNMs play an important role not only in material properties but also in the determination of how materials interact at the nano-bio interface. In this article, we probed the influence of defect-induced hydrophilicity on the biocorona formation using micro-Raman, photoluminescence, infrared spectroscopy, electrochemistry, and molecular dynamics simulations. Our results show that the interaction of proteins (albumin and fibrinogen) with CNMs is strongly influenced by charge-transfer between them, inducing protein unfolding which enhances conformational entropy and higher protein adsorption.

SUBMITTER: Sengupta B

PROVIDER: S-EPMC4751053 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Influence of carbon nanomaterial defects on the formation of protein corona.

Sengupta Bishwambhar B Gregory Wren E WE Zhu Jingyi J Dasetty Siva S Karakaya Mehmet M Brown Jared M JM Rao Apparao M AM Barrows John K JK Sarupria Sapna S Podila Ramakrishna R

RSC advances 20150923 100

In any physiological media, carbon nanomaterials (CNM) strongly interact with biomolecules leading to the formation of biocorona, which subsequently dictate the physiological response and the fate of CNMs. Defects in CNMs play an important role not only in material properties but also in the determination of how materials interact at the nano-bio interface. In this article, we probed the influence of defect-induced hydrophilicity on the biocorona formation using micro-Raman, photoluminescence, i ...[more]

PMID: 26877870

Similar Datasets

Formation and cell translocation of carbon nanotube-fibrinogen protein corona.

Project description:The binding of plasma fibrinogen with both single-walled and multi-walled carbon nanotubes (SWNTs and MWNTs) has been examined. Specifically, our absorbance study indicated that MWNTs were coated with multi-layers of fibrinogen to render a "hard protein corona," while SWNTs were adsorbed with thin layers of the protein to precipitate out of the aqueous phase. In addition, static quenching as a result of energy transfer from fluorescently labeled fibrinogen to their nanotube substrates was revealed by Stern-Volmer analysis. When exposed to HT-29 cells, the nanotubes and fibrinogen could readily dissociate, possibly stemming from their differential affinities for the amphiphilic membrane bilayer.

| S-EPMC3470598 | biostudies-other

Probing protein dissociation from gold nanoparticles and the influence of temperature from the protein corona formation mechanism.

Project description:Gold nanoparticles (AuNPs) provide a novel approach for protein enrichment and analysis due to their protein adsorption properties, forming a so called protein corona. This corona can significantly influence the protein's structure and characteristics, hindering their identification in situ. Dissociation is an important solution to analyze and identify the composition of protein coronas. However, a comprehensive picture of adsorbed protein dissociation is lacking. In this study, the protein dissociation from the protein corona and influencing factors were investigated on the basis of the formation mechanism and time evolution. Temperature and cysteine are the key factors influencing protein dissociation by altering the protein's binding ability. The results showed that half Au-S formation time is an important time point for thio-protein dissociation by the method of high speed centrifugation. When incubated for longer than that time, the thio-protein located in the hard corona could only be separated by β-mercaptoethanol replacement under analytical ultracentrifugation. However, Fourier-transform infrared spectroscopy (FTIR) revealed significant changes that occurred in βlg's secondary structure after ultracentrifugation. The Au-S bond formation time offers the potential to define the protein enrichment time of AuNPs.

| S-EPMC9033426 | biostudies-literature

Understanding the Influence of a Bifunctional Polyethylene Glycol Derivative in Protein Corona Formation around Iron Oxide Nanoparticles.

Project description:Superparamagnetic iron oxide nanoparticles are one of the most prominent agents used in theranostic applications, with MRI imaging the main application assessed. The biomolecular interface formed on the surface of a nanoparticle in a biological medium determines its behaviour in vitro and in vivo. In this study, we have compared the formation of the protein corona on highly monodisperse iron oxide nanoparticles with two different coatings, dimercaptosuccinic acid (DMSA), and after conjugation, with a bifunctional polyethylene glycol (PEG)-derived molecule (2000 Da) in the presence of Wistar rat plasma. The protein fingerprints around the nanoparticles were analysed in an extensive proteomic study. The results presented in this work indicate that the composition of the protein corona is very difficult to predict. Proteins from different functional categories-cell components, lipoproteins, complement, coagulation, immunoglobulins, enzymes and transport proteins-were identified in all samples with very small variability. Although both types of nanoparticles have similar amounts of bonded proteins, very slight differences in the composition of the corona might explain the variation observed in the uptake and biotransformation of these nanoparticles in Caco-2 and RAW 264.7 cells. Cytotoxicity was also studied using a standard 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide assay. Controlling nanoparticles' reactivity to the biological environment by deciding on its surface functionalization may suggest new routes in the control of the biodistribution, biodegradation and clearance of multifunctional nanomedicines.

| S-EPMC6678275 | biostudies-literature

Understanding the Kinetics of Protein-Nanoparticle Corona Formation.

Project description:When a pristine nanoparticle (NP) encounters a biological fluid, biomolecules spontaneously form adsorption layers around the NP, called "protein corona". The corona composition depends on the time-dependent environmental conditions and determines the NP's fate within living organisms. Understanding how the corona evolves is fundamental in nanotoxicology as well as medical applications. However, the process of corona formation is challenging due to the large number of molecules involved and to the large span of relevant time scales ranging from 100 μs, hard to probe in experiments, to hours, out of reach of all-atoms simulations. Here we combine experiments, simulations, and theory to study (i) the corona kinetics (over 10-3-103 s) and (ii) its final composition for silica NPs in a model plasma made of three blood proteins (human serum albumin, transferrin, and fibrinogen). When computer simulations are calibrated by experimental protein-NP binding affinities measured in single-protein solutions, the theoretical model correctly reproduces competitive protein replacement as proven by independent experiments. When we change the order of administration of the three proteins, we observe a memory effect in the final corona composition that we can explain within our model. Our combined experimental and computational approach is a step toward the development of systematic prediction and control of protein-NP corona composition based on a hierarchy of equilibrium protein binding constants.

| S-EPMC5391497 | biostudies-literature

Exploring Carbon Nanomaterial Diversity for Nucleation of Protein Crystals.

Project description:Controlling crystal nucleation is a crucial step in obtaining high quality protein crystals for structure determination by X-ray crystallography. Carbon nanomaterials (CNMs) including carbon nanotubes, graphene oxide, and carbon black provide a range of surface topographies, porosities and length scales; functionalisation with two different approaches, gas phase radical grafting and liquid phase reductive grafting, provide routes to a range of oligomer functionalised products. These grafted materials, combined with a range of controls, were used in a large-scale assessment of the effectiveness for protein crystal nucleation of 20 different carbon nanomaterials on five proteins. This study has allowed a direct comparison of the key characteristics of carbon-based nucleants: appropriate surface chemistry, porosity and/or roughness are required. The most effective solid system tested in this study, carbon black nanoparticles functionalised with poly(ethylene glycol) methyl ether of mean molecular weight 5000, provides a novel highly effective nucleant, that was able to induce crystal nucleation of four out of the five proteins tested at metastable conditions.

| S-EPMC4740738 | biostudies-other

Experimental conditions influence the formation and composition of the corona around gold nanoparticles.

Project description:BackgroundOvarian cancer is one of the deadliest gynecological malignancies. While the overall survival of ovarian cancer patients has slightly improved in recent years in the developed world, it remains clinically challenging due to its frequent late diagnosis and the lack of reliable diagnostic and/or prognostic markers. The aim of this study was to identify potential new molecular target proteins (NMTPs) responsible for the poor outcomes. When nanoparticles (NP) are exposed to biological fluids, a protein coat, termed the protein corona (PC), forms around the NP, and the PC represents a tool to identify NMTPs. This study investigates the influence of pre-processing conditions, such as lysis conditions and serum/plasma treatment, on the PC composition and the resulting identification of NMTPs.ResultsUsing gel electrophoresis, pre-processing conditions, including cell-lysis techniques and enrichment of low-abundance proteins (LAPs) by immunocentrifugation of serum/plasma, were shown to alter the relative amounts and compositions of proteins. PCs formed when 20 nm gold-NPs (GNPs) were incubated with lysate proteins from either RIPA- or urea lysis. Proteomic analysis of these PCs showed 2-22-fold enrichment of NMTPs in PCs from urea lysates as compared to RIPA lysates. Enriched NMTPs were then classified as cellular components, biological and molecular functions-associated proteins. The impact of enriched LAPs (eLAPs) on both PC composition and NMTP identification was shown by comparative proteomic analysis of original plasma, eLAPs, and PCs derived from eLAPs; eLAPs-PCs enhanced the abundance of NMTPs approximately 13%. Several NMTPs, including gasdermin-B, dermcidin, and kallistatin, were identified by this method demonstrating the potential use of this PC approach for molecular target discovery.ConclusionThe current study showed that the pre-processing conditions modulate PC composition and can be used to enhance identification of NMTPs.

| S-EPMC7788026 | biostudies-literature

Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity.

Project description:Physiochemical properties of engineered nanoparticles (NPs) play a vital role in nano-bio interactions, which are critical for nanotoxicity and nanomedicine research. To understand the effects of NP hydrophobicity on the formation of the protein corona, we synthesized four gold NPs with a continuous change in hydrophobicity ranging from -2.6 to 2.4. Hydrophobic NPs adsorbed 2.1-fold proteins compared to hydrophilic ones. Proteins with small molecular weights (<50 kDa) and negatively charge (PI < 7) constituted the majority of the protein corona, especially for hydrophobic NPs. Moreover, proteins preferred binding to hydrophilic NPs (vitronectin and antithrombin III), hydrophobic NPs (serum albumin and hemoglobin fetal subunit beta), and medium hydrophobic NPs (talin 1 and prothrombin) were identified. Besides, proteins such as apolipoprotein bound to all NPs, did not show surface preference. We also found that there was a dynamic exchange between hard protein corona and solution proteins. Because of such dynamic exchanges, protein-bound NPs could expose their surface in biological systems. Hydrophilic NPs exhibited higher protein exchange rate than hydrophobic NPs. Above understandings have improved our capabilities to modulate protein corona formation by controlling surface chemistry of NPs. These will also help modulate nanotoxicity and develop better nanomedcines.

| S-EPMC7100549 | biostudies-literature

Nanoparticles Surface Chemistry Influence on Protein Corona Composition and Inflammatory Responses.

Project description:Nanoparticles are widely used for biomedical applications such as vaccine, drug delivery, diagnostics, and therapeutics. This study aims to reveal the influence of nanoparticle surface functionalization on protein corona formation from blood serum and plasma and the subsequent effects on the innate immune cellular responses. To achieve this goal, the surface chemistry of silica nanoparticles of 20 nm diameter was tailored via plasma polymerization with amine, carboxylic acid, oxazolines, and alkane functionalities. The results of this study show significant surface chemistry-induced differences in protein corona composition, which reflect in the subsequent inflammatory consequences. Nanoparticles rich with carboxylic acid surface functionalities increased the production of pro-inflammatory cytokines in response to higher level of complement proteins and decreased the number of lipoproteins found in their protein coronas. On another hand, amine rich coatings led to increased expressions of anti-inflammatory markers such as arginase. The findings demonstrate the potential to direct physiological responses to nanomaterials via tailoring their surface chemical composition.

| S-EPMC8879273 | biostudies-literature

Best practice in reporting corona studies: Minimum information about Nanomaterial Biocorona Experiments (MINBE).

Project description:Characterisation of the adsorption of biomolecules, or a biocorona, on nanomaterials has proliferated in the past 10 years, as protein corona studies provide molecular level insight into mechanisms of cellular recognition, uptake, and toxicity of nanomaterials. At the crossroads of two rapidly evolving orthogonal fields, nanoscience and proteomics, the interdisciplinarity of protein corona studies creates challenges for experimental design and reporting. Here we propose a flexible checklist for experimental design and reporting guidelines to outline Minimum Information about Nanomaterial Biocorona Experiments (MINBE). The checklist for experimental design, compiled after review of reporting within the protein corona literature, provides researchers with prompts to ensure best practice experimental approaches for each stage of the workflow, collated from the nanoscience, proteomics, and bioinformatics fields. Reporting guidelines are also assembled from established sources, integrated to span the entire workflow and extended and modified to aid interdisciplinary researchers in the most challenging stages of the workflow. Where appropriate, de novo guidelines to address areas specific to protein corona studies, including exposure conditions and isolation of adsorbed proteins, were written. The MINBE guidelines provide protein corona researchers with a conduit between materials science techniques and proteomics. Implementation of these guidelines is anticipated to catalyse enhanced quality, impact, and extent of data mining and computational modelling of protein corona composition and its role in nanosafety and nanomedicine. Furthermore, high quality experimental design and reporting in the bio-nanosciences will enhance the next phase of targeted nanomedicines and sustainable nanotechnologies.

| S-EPMC7405976 | biostudies-literature

Biological Impacts of Reduced Graphene Oxide Affected by Protein Corona Formation.

Project description:Applications of reduced graphene oxide (rGO) in many different areas have been gradually increasing owing to its unique physicochemical characteristics, demanding more understanding of their biological impacts. Herein, we assessed the toxicological effects of rGO in mammary epithelial cells. Because the as-synthesized rGO was dissolved in sodium cholate to maintain a stable aqueous dispersion, we hypothesize that changing the cholate concentration in the dispersion may alter the surface property of rGO and subsequently affect its cellular toxicity. Thus, four types of rGO were prepared and compared: rGO dispersed in 4 and 2 mg/mL sodium cholate, labeled as rGO and concentrated-rGO (c-rGO), respectively, and rGO and c-rGO coated with a protein corona through 1 h incubation in culture media, correspondingly named pro-rGO and pro-c-rGO. Notably, c-rGO and pro-c-rGO exhibited higher toxicity than rGO and pro-rGO and also caused higher reactive oxygen species production, more lipid membrane peroxidation, and more significant disruption of mitochondrial-based ATP synthesis. In all toxicological assessments, pro-c-rGO induced more severe adverse impacts than c-rGO. Further examination of the material surface, protein adsorption, and cellular uptake showed that the surface of c-rGO was coated with a lower content of surfactant and adsorbed more proteins, which may result in the higher cellular uptake observed with pro-c-rGO than pro-rGO. Several proteins involved in cellular redox mediation were also more enriched in pro-c-rGO. These results support the strong correlation between dispersant coating and corona formation and their subsequent cellular impacts. Future studies in this direction could reveal a deeper understanding of the correlation and the specific cellular pathways involved and help gain knowledge on how the toxicity of rGO could be modulated through surface modification, guiding the sustainable applications of rGO.

| S-EPMC9842398 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data