Sensing nanoparticle-protein corona using nanoparticle enhanced Laser Induced Breakdown Spectroscopy signal enhancement

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F21%3APU142018" target="_blank" >RIV/00216305:26620/21:PU142018 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0039914021006627" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0039914021006627</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.talanta.2021.122741" target="_blank" >10.1016/j.talanta.2021.122741</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Sensing nanoparticle-protein corona using nanoparticle enhanced Laser Induced Breakdown Spectroscopy signal enhancement

Popis výsledku v původním jazyce

Recently nanoparticle enhanced Laser Induced Breakdown Spectroscopy (NELIBS) is getting a growing interest as an effective alternative method for improving the analytical performance of LIBS. On the other hand, the plasmonic effect during laser ablation can be used for a different task rather than elemental analysis. In this paper, the dependence of NELIBS emission signal enhancement on nanoparticle-protein solutions dried on a reference substrate (metallic titanium) was investigated. Two proteins were studied: Human Serum Albumin (HSA) and Cytochrome C (CytC). Both proteins have a strong affinity for the gold nanoparticles (AuNPs) due to the bonding between the single free exterior thiol (associated with a cysteine residue) and the gold surface to form a stable protein corona. Then, since the protein sizes are vastly different, a different number of protein units is needed to cover AuNP surface to form a protein layer. The NP-protein solution was dropped and dried onto the titanium substrate. Then the NELIBS signal enhancement of Ti emission lines was correlated to the solution characteristics as determined with Dynamic Light Scattering (DLS), Surface Plasmon Resonance (SPR) spectroscopy and Laser Doppler Electrophoresis (LDE) for zeta-potential determination. Moreover, the dried solutions were studied with TEM (Transmission Electron Microscopy) for the inspection of the inter-particle distance. The structural effect of the NP-protein conjugates on the NELIBS signal reveals that NELIBS can be used to determine the number of protein units required to form the nanoparticle-protein corona with good accuracy. Although the investigated NP-protein systems are simple cases in biological applications, this work demonstrates, for the first time, a different use of NELIBS that is beyond elemental analysis and it opens the way for sensing the nanoparticle protein corona.

Název v anglickém jazyce

Sensing nanoparticle-protein corona using nanoparticle enhanced Laser Induced Breakdown Spectroscopy signal enhancement

Popis výsledku anglicky

Recently nanoparticle enhanced Laser Induced Breakdown Spectroscopy (NELIBS) is getting a growing interest as an effective alternative method for improving the analytical performance of LIBS. On the other hand, the plasmonic effect during laser ablation can be used for a different task rather than elemental analysis. In this paper, the dependence of NELIBS emission signal enhancement on nanoparticle-protein solutions dried on a reference substrate (metallic titanium) was investigated. Two proteins were studied: Human Serum Albumin (HSA) and Cytochrome C (CytC). Both proteins have a strong affinity for the gold nanoparticles (AuNPs) due to the bonding between the single free exterior thiol (associated with a cysteine residue) and the gold surface to form a stable protein corona. Then, since the protein sizes are vastly different, a different number of protein units is needed to cover AuNP surface to form a protein layer. The NP-protein solution was dropped and dried onto the titanium substrate. Then the NELIBS signal enhancement of Ti emission lines was correlated to the solution characteristics as determined with Dynamic Light Scattering (DLS), Surface Plasmon Resonance (SPR) spectroscopy and Laser Doppler Electrophoresis (LDE) for zeta-potential determination. Moreover, the dried solutions were studied with TEM (Transmission Electron Microscopy) for the inspection of the inter-particle distance. The structural effect of the NP-protein conjugates on the NELIBS signal reveals that NELIBS can be used to determine the number of protein units required to form the nanoparticle-protein corona with good accuracy. Although the investigated NP-protein systems are simple cases in biological applications, this work demonstrates, for the first time, a different use of NELIBS that is beyond elemental analysis and it opens the way for sensing the nanoparticle protein corona.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Talanta

ISSN

0039-9140

e-ISSN

1873-3573

Svazek periodika

235

Číslo periodika v rámci svazku

122741

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

1-8

Kód UT WoS článku

000701191200002

EID výsledku v databázi Scopus

2-s2.0-85111684392