Time evolution of β-lactoglobulin corona formation on gold nanoparticles and impact on allergy

2020 ◽  
Author(s):  
Xiaoning Zhang ◽  
Meifeng Li ◽  
Yuanping Lv ◽  
Xiaoling Sun ◽  
Yao Han ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Secondary Structure ◽  
Time Evolution ◽  
Electrostatic Force ◽  
Protein Corona ◽  
Raw Milk ◽  
Covalent Bonds ◽  
Corona Formation ◽  
Β Lactoglobulin ◽  
Β Sheet

Abstract Gold nanoparticles (AuNPs) are modified immediately by the adsorption of β-lactoglobulin (βlg) when designed as colorimetric probe in raw milk, leading to the formation of a protein corona. This adsorption results mainly from a fast electrostatic force and a slow formation of Au-S covalent bonds, which is a precondition for the use of AuNPs in biodetection. The proteins corona influences the structure and bioactivity of adsorbed protein, such as the allergy. In this study, the mechanism of βlg adsorbed on AuNPs was investigated in terms of stoichiometry, binding affinity (Ka), time evolution of Au-S bond, and general secondary structure changes to address the desensitization of AuNPs. The results show that about 3,600 βlg are adsorbed on a single AuNPs, and the Ka is 2.9 ± 0.7 × 10 6 M -1 . The formation of Au-S bonds takes about 9 h, which is the time needed for complete changes in secondary structure and the IgE combining capacity. The structure of allergenic epitopes assigned to β-sheet was destroyed by the formation of Au-S bond, then induced to the decrease allergy. Furthermore, Fourier transform infrared spectroscopy confirmed a decrease in β-sheet contents after conjugated with AuNPs.

scholarly journals Experimental and Computational Investigation of the Structure of Peptide Monolayers on Gold Nanoparticles

2016 ◽  
Author(s):  
Elena Colangelo ◽  
Qiubo Chen ◽  
Adam M. Davidson ◽  
David Paramelle ◽  
Michael B. Sullivan ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Secondary Structure ◽  
Small Molecules ◽  
Self Assembly ◽  
Gold Surface ◽  
Biochemical Properties ◽  
Computational Investigation ◽  
Predictive Tool ◽  
Dynamics Simulations ◽  
Β Sheet

ABSTRACTThe self-assembly and self-organization of small molecules at the surface of nanoparticles constitute a potential route towards the preparation of advanced protein-like nanosystems. However, their structural characterization, critical to the design of bio-nanomaterials with well-defined biophysical and biochemical properties, remains highly challenging. Here, a computational model for peptide-capped gold nanoparticles is developed using experimentally characterized CALNN-and CFGAILSS-capped gold nanoparticles as a benchmark. The structure of CALNN and CFGAILSS monolayers is investigated by both structural biology techniques and molecular dynamics simulations. The calculations reproduce the experimentally observed dependence of the monolayer secondary structure on peptide capping density and on nanoparticle size, thus giving us confidence in the model. Furthermore, the computational results reveal a number of new features of peptide-capped monolayers, including the importance of sulfur movement for the formation of secondary structure motifs, the presence of water close to the gold surface even in tightly packed peptide monolayers, and the existence of extended 2D parallel β-sheet domains in CFGAILSS monolayers. The model developed here provides a predictive tool that may assist in the design of further bio-nanomaterials.

scholarly journals Gold Nanostars with Reduced Fouling Facilitate Small Molecule Detection in the Presence of Protein

Nanomaterials ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 2565
Author(s):  
Anastasiia Tukova ◽  
Inga Christine Kuschnerus ◽  
Alfonso Garcia-Bennett ◽  
Yuling Wang ◽  
Alison Rodger
Keyword(s):  
Gold Nanoparticles ◽  
Small Molecule ◽  
Protein Corona ◽  
Surface Enhanced Raman Spectroscopy ◽  
Biological Media ◽  
Gold Nanostars ◽  
Cellular Environment ◽  
Vis Spectroscopy ◽  
Corona Formation

Gold nanoparticles have the potential to be used in biomedical applications from diagnostics to drug delivery. However, interactions of gold nanoparticles with different biomolecules in the cellular environment result in the formation of a “protein corona”—a layer of protein formed around a nanoparticle, which induces changes in the properties of nanoparticles. In this work we developed methods to reproducibly synthesize spheroidal and star-shaped gold nanoparticles, and carried out a physico-chemical characterization of synthesized anionic gold nanospheroids and gold nanostars through transmission electron microscopy (TEM), dynamic light scattering (DLS), zeta potential (ZP), nanoparticles tracking analysis (NTA), ultraviolet-visible (UV–Vis) spectroscopy and estimates of surface-enhanced Raman spectroscopy (SERS) signal enhancement ability. We analyzed how they interact with proteins after pre-incubation with bovine serum albumin (BSA) via UV–Vis, DLS, ZP, NTA, SERS, cryogenic TEM (cryo-TEM) and circular dichroism (CD) spectroscopy. The tests demonstrated that the protein adsorption on the particles’ surfaces was different for spheroidal and star shaped particles. In our experiments, star shaped particles limited the protein corona formation at SERS “hot spots”. This benefits the small-molecule sensing of nanostars in biological media. This work adds more understanding about protein corona formation on gold nanoparticles of different shapes in biological media, and therefore guides design of particles for studies in vitro and in vivo.

scholarly journals Reversible Control of Protein Corona Formation on Gold Nanoparticles Using Host–Guest Interactions

ACS Nano ◽  
2020 ◽  
Vol 14 (5) ◽  
pp. 5382-5391 ◽  
Author(s):  
Jesús Mosquera ◽  
Isabel García ◽  
Malou Henriksen-Lacey ◽  
Miguel Martínez-Calvo ◽  
Mónica Dhanjani ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Protein Corona ◽  
Corona Formation

Aggregation and protein corona formation on gold nanoparticles affect viability and liver functions of primary rat hepatocytes

Nanomedicine ◽  
2016 ◽  
Vol 11 (17) ◽  
pp. 2275-2287 ◽  
Author(s):  
Wee Ling Koh ◽  
Phoebe Huijun Tham ◽  
Hanry Yu ◽  
Hwa Liang Leo ◽  
James Chen Yong Kah
Keyword(s):  
Gold Nanoparticles ◽  
Rat Hepatocytes ◽  
Protein Corona ◽  
Primary Rat Hepatocytes ◽  
Corona Formation ◽  
Liver Functions

Alterations in nanoparticle protein corona by biological surfactants: Impact of bile salts on β-lactoglobulin-coated gold nanoparticles

2014 ◽  
Vol 426 ◽  
pp. 333-340 ◽  
Author(s):  
Thunnalin Winuprasith ◽  
Sirinya Chantarak ◽  
Manop Suphantharika ◽  
Lili He ◽  
David Julian McClements
Keyword(s):  
Gold Nanoparticles ◽  
Bile Salts ◽  
Protein Corona ◽  
Β Lactoglobulin

Component-Specific Analysis of Plasma Protein Corona Formation on Gold Nanoparticles Using Multiplexed Surface Plasmon Resonance

Small ◽  
2015 ◽  
Vol 12 (9) ◽  
pp. 1174-1182 ◽  
Author(s):  
Abhijeet Patra ◽  
Tao Ding ◽  
Gokce Engudar ◽  
Yi Wang ◽  
Michal Marcin Dykas ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasma Protein ◽  
Plasmon Resonance ◽  
Protein Corona ◽  
Specific Analysis ◽  
Corona Formation

scholarly journals Reducing Protein Corona Formation and Enhancing Colloidal Stability of Gold Nanoparticles by Capping with Silica Monolayers

2018 ◽  
Vol 31 (1) ◽  
pp. 57-61 ◽  
Author(s):  
Jesús Mosquera ◽  
Isabel García ◽  
Malou Henriksen-Lacey ◽  
Guillermo González-Rubio ◽  
Luis M. Liz-Marzán
Keyword(s):  
Gold Nanoparticles ◽  
Colloidal Stability ◽  
Protein Corona ◽  
Corona Formation

scholarly journals In vivo formation of protein corona on gold nanoparticles. The effect of their size and shape

Nanoscale ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 1256-1264 ◽  
Author(s):  
Rafaela García-Álvarez ◽  
Marilena Hadjidemetriou ◽  
Ana Sánchez-Iglesias ◽  
Luis M. Liz-Marzán ◽  
Kostas Kostarelos
Keyword(s):  
Gold Nanoparticles ◽  
Blood Circulation ◽  
Protein Corona ◽  
Size And Shape ◽  
Corona Formation ◽  
Anisotropic Gold Nanoparticles

A detailed study is presented of in vivo protein corona formation on anisotropic gold nanoparticles, after blood circulation in mice.

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

RSC Advances ◽  
2021 ◽  
Vol 11 (30) ◽  
pp. 18198-18204
Author(s):  
Meifeng Li ◽  
Xiaoning Zhang ◽  
Sining Li ◽  
Xiaoqing Shao ◽  
Huixian Chen ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Formation Mechanism ◽  
Protein Corona ◽  
Influence Of Temperature ◽  
Corona Formation ◽  
Important Solution ◽  
Protein Dissociation

A protein corona changes protein's structure and characteristics, hindering their identification in situ. Dissociation is an important solution to identify their composition.

A Study of the Amide III Band by FT-IR Spectrometry of the Secondary Structure of Albumin, Myoglobin, and γ-Globulin

1987 ◽  
Vol 41 (2) ◽  
pp. 180-184 ◽  
Author(s):  
Koichi Kaiden ◽  
Tomoko Matsui ◽  
Shigeyuki Tanaka
Keyword(s):  
Secondary Structure ◽  
Conformational Changes ◽  
Phosphate Buffer Solution ◽  
Heat Denaturation ◽  
Buffer Solution ◽  
Ir Spectrometry ◽  
Ft Ir ◽  
Α Helix ◽  
Β Lactoglobulin ◽  
Β Sheet

FT-IR spectrometry was applied to the identification of the secondary structure species of a living protein. The spectra of native myoglobin and albumin were obtained with methods using either KBr pellet or film formed on a KBr window from an aqueous solution. Pellet preparation of myoglobin and albumin caused the structure to change from α-helix to β-structure. The conformational changes that arise from heat denaturation of myoglobin, albumin, and γ-globulin were observed by the changes in the amide I, II, and III bands. The bands of the 1300, 1260, and 1235 cm−1 regions were respectively assigned to α-helix, disordered, and β-sheet structures. These band positions were substantiated by the spectra of β-lactoglobulin and α-casein. α-Helix structure probably changes to β-structure in the presence of alkali halide, and changes to disordered structure with heat denaturation in phosphate buffer solution. The secondary structure of a protein is further identified by use of the information obtained from the amide I, II, and III bands; the amide III band is especially important. Furthermore, it may be possible to characterize the species of secondary structures of proteins adsorbed on material surfaces.

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