Engineered protein-iron and/or gold-protein-iron nanocomposites in aqueous solutions upon UVA light: Photo-induced electron transfer possibilities and limitations

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15640%2F24%3A73624553" target="_blank" >RIV/61989592:15640/24:73624553 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/24:73624553

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S1010603023008808?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1010603023008808?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jphotochem.2023.115415" target="_blank" >10.1016/j.jphotochem.2023.115415</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Engineered protein-iron and/or gold-protein-iron nanocomposites in aqueous solutions upon UVA light: Photo-induced electron transfer possibilities and limitations

Popis výsledku v původním jazyce

Occurrence/suppression of photo-induced electron transfer (PI -ET) process in solutions of nanocomposites represents a very hot topic in several photo-related research domains. In this work, this phenomenon is investigated in aqueous solutions using iron-containing mono-/bi-metallic nanocomposites that have been engineered through protein-templated syntheses, with the aim to potentially create new biocompatible imaging contrast agents for medical diagnostics. Two types of iron-containing nanocomposites, mono-metallic (protein -Fe) and bimetallic (Au -protein -Fe), have been synthesized and characterized with the aid of several experimental techniques, such as high-resolution transmission electron microscopy (HR -TEM), steady -state fluorescence, electron paramagnetic resonance (EPR) and light-induced EPR (LEPR). Theoretical model of the N -terminal region of the bovine serum albumin protein interacting with Fe cations and simulations of the EPR spectral features upon UVA light irradiation complemented the material&apos;s analysis. Two iron forms within the mono-/bi-metallic nanocomposites have been detected experimentally: (i) complexed iron cations (giving EPR signal at g = 4.29) and (ii) superparamagnetic iron oxide nanoparticles (SPIONs; expressing EPR resonances at g// = 2.21 and g perpendicular to = 2.09). Upon UVA-light irradiation (325 nm), PI -ET between the two iron forms have been observed in the protein -Fe nanocomposite; however, this electronic communication is suppressed in the Au -protein -Fe system. The presence of luminescent Au nanoclusters and dissimilar sizes of SPIONs in bi-metallic nanocomposites (around 5 nm vs. approx. 2 nm in the monometallic protein -Fe system) represent the two possible reasons underneath suppression of the PI -ET process in the former. Moreover, center dot OH radicals were detected in aqueous solutions in both iron-containing nanocomposites (Fe and Au/Fe systems) when irradiated at 325 nm for 5 min at r. t. The reported evidence of PI -ET in iron-containing nanocomposite aqueous solutions can thus have a large impact on their potential medical and/or environmental applications.

Název v anglickém jazyce

Engineered protein-iron and/or gold-protein-iron nanocomposites in aqueous solutions upon UVA light: Photo-induced electron transfer possibilities and limitations

Popis výsledku anglicky

Occurrence/suppression of photo-induced electron transfer (PI -ET) process in solutions of nanocomposites represents a very hot topic in several photo-related research domains. In this work, this phenomenon is investigated in aqueous solutions using iron-containing mono-/bi-metallic nanocomposites that have been engineered through protein-templated syntheses, with the aim to potentially create new biocompatible imaging contrast agents for medical diagnostics. Two types of iron-containing nanocomposites, mono-metallic (protein -Fe) and bimetallic (Au -protein -Fe), have been synthesized and characterized with the aid of several experimental techniques, such as high-resolution transmission electron microscopy (HR -TEM), steady -state fluorescence, electron paramagnetic resonance (EPR) and light-induced EPR (LEPR). Theoretical model of the N -terminal region of the bovine serum albumin protein interacting with Fe cations and simulations of the EPR spectral features upon UVA light irradiation complemented the material&apos;s analysis. Two iron forms within the mono-/bi-metallic nanocomposites have been detected experimentally: (i) complexed iron cations (giving EPR signal at g = 4.29) and (ii) superparamagnetic iron oxide nanoparticles (SPIONs; expressing EPR resonances at g// = 2.21 and g perpendicular to = 2.09). Upon UVA-light irradiation (325 nm), PI -ET between the two iron forms have been observed in the protein -Fe nanocomposite; however, this electronic communication is suppressed in the Au -protein -Fe system. The presence of luminescent Au nanoclusters and dissimilar sizes of SPIONs in bi-metallic nanocomposites (around 5 nm vs. approx. 2 nm in the monometallic protein -Fe system) represent the two possible reasons underneath suppression of the PI -ET process in the former. Moreover, center dot OH radicals were detected in aqueous solutions in both iron-containing nanocomposites (Fe and Au/Fe systems) when irradiated at 325 nm for 5 min at r. t. The reported evidence of PI -ET in iron-containing nanocomposite aqueous solutions can thus have a large impact on their potential medical and/or environmental applications.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY

ISSN

1010-6030

e-ISSN

1873-2666

Svazek periodika

450

Číslo periodika v rámci svazku

May

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

001155889100001

EID výsledku v databázi Scopus

2-s2.0-85181754721