Size- and surface functionalization-driven molecular interaction of CdSe quantum dots with jack bean urease: multispectroscopic, thermodynamic, and AFM approach

Quantum dots (QDs) with distinctive optical properties have been extensively researched and developed for usage in solar cells, imaging, drug delivery, cellular targeting, etc. But the inevitable production of QDs can lead to their unavoidable release and increased environmental concentration. Depen...

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Veröffentlicht in:Environmental science and pollution research international 2023-04, Vol.30 (16), p.48300-48322
Hauptverfasser: Gupta, Jagriti, Rajamani, Paulraj
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description Quantum dots (QDs) with distinctive optical properties have been extensively researched and developed for usage in solar cells, imaging, drug delivery, cellular targeting, etc. But the inevitable production of QDs can lead to their unavoidable release and increased environmental concentration. Depending on morphological and surface properties, QDs at the nano-bio interface considerably impact the activity and structure of bio-molecules. The present study investigates the interaction of metalloenzyme jack bean urease (JBU) and bi-sized CdSe QDs (2.43 nm and 3.63 nm), surface-functionalized to mercaptopropionic acid (MPA) (–COOH), l -cysteine (CYS), l -glutathione (GSH), N-acetyl l -cysteine (NAC) (–COOH, –NH 2 ), and cysteamine hydrochloride (CYST) (–NH 2 ) to assess any alterations in JBU’s binding, microenvironment, structure, exciton lifetime, and activity. JBU catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide; any changes in its properties could threaten the survival of several microbes and plants. Spectroscopy techniques such as UV–Vis, fluorescence, circular dichroism, synchronous, time-resolved fluorescence, atomic force microscopy, and JBU activity assay were studied. Results suggested highly spontaneous and energy-favored interactions, which involved static quenching and hydrophobic forces of varied magnitude, dependent on QDs properties. The size, surface modifications, and dosage of QDs significantly impacted the secondary structure and activity of JBUs. Even though the larger sizes of the relevant modifications demonstrated stronger binding, the smaller sizes had the greatest impact on α-helicity and activity. CYST-capped QDs with an average number of the binding site ( n ) = 1, reduced α-helicity by 16% and activity by 22–30% at 7 nM concentration. In contrast, MPA-capped QDs with n  
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Depending on morphological and surface properties, QDs at the nano-bio interface considerably impact the activity and structure of bio-molecules. The present study investigates the interaction of metalloenzyme jack bean urease (JBU) and bi-sized CdSe QDs (2.43 nm and 3.63 nm), surface-functionalized to mercaptopropionic acid (MPA) (–COOH), l -cysteine (CYS), l -glutathione (GSH), N-acetyl l -cysteine (NAC) (–COOH, –NH 2 ), and cysteamine hydrochloride (CYST) (–NH 2 ) to assess any alterations in JBU’s binding, microenvironment, structure, exciton lifetime, and activity. JBU catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide; any changes in its properties could threaten the survival of several microbes and plants. Spectroscopy techniques such as UV–Vis, fluorescence, circular dichroism, synchronous, time-resolved fluorescence, atomic force microscopy, and JBU activity assay were studied. Results suggested highly spontaneous and energy-favored interactions, which involved static quenching and hydrophobic forces of varied magnitude, dependent on QDs properties. The size, surface modifications, and dosage of QDs significantly impacted the secondary structure and activity of JBUs. Even though the larger sizes of the relevant modifications demonstrated stronger binding, the smaller sizes had the greatest impact on α-helicity and activity. CYST-capped QDs with an average number of the binding site ( n ) = 1, reduced α-helicity by 16% and activity by 22–30% at 7 nM concentration. In contrast, MPA-capped QDs with n  &lt; 1 had the least effect on α-helical structure and activity. The smaller GSH-capped QDs increased the activity by 9%, via partially restoring JBU’s α-helical content. The study thus thoroughly analyzed the impact of varied-size and surface-functionalized QDs on the structure and function of JBU, which can be exploited further for several biomedical applications. 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Results suggested highly spontaneous and energy-favored interactions, which involved static quenching and hydrophobic forces of varied magnitude, dependent on QDs properties. The size, surface modifications, and dosage of QDs significantly impacted the secondary structure and activity of JBUs. Even though the larger sizes of the relevant modifications demonstrated stronger binding, the smaller sizes had the greatest impact on α-helicity and activity. CYST-capped QDs with an average number of the binding site ( n ) = 1, reduced α-helicity by 16% and activity by 22–30% at 7 nM concentration. In contrast, MPA-capped QDs with n  &lt; 1 had the least effect on α-helical structure and activity. The smaller GSH-capped QDs increased the activity by 9%, via partially restoring JBU’s α-helical content. The study thus thoroughly analyzed the impact of varied-size and surface-functionalized QDs on the structure and function of JBU, which can be exploited further for several biomedical applications. 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Depending on morphological and surface properties, QDs at the nano-bio interface considerably impact the activity and structure of bio-molecules. The present study investigates the interaction of metalloenzyme jack bean urease (JBU) and bi-sized CdSe QDs (2.43 nm and 3.63 nm), surface-functionalized to mercaptopropionic acid (MPA) (–COOH), l -cysteine (CYS), l -glutathione (GSH), N-acetyl l -cysteine (NAC) (–COOH, –NH 2 ), and cysteamine hydrochloride (CYST) (–NH 2 ) to assess any alterations in JBU’s binding, microenvironment, structure, exciton lifetime, and activity. JBU catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide; any changes in its properties could threaten the survival of several microbes and plants. Spectroscopy techniques such as UV–Vis, fluorescence, circular dichroism, synchronous, time-resolved fluorescence, atomic force microscopy, and JBU activity assay were studied. Results suggested highly spontaneous and energy-favored interactions, which involved static quenching and hydrophobic forces of varied magnitude, dependent on QDs properties. The size, surface modifications, and dosage of QDs significantly impacted the secondary structure and activity of JBUs. Even though the larger sizes of the relevant modifications demonstrated stronger binding, the smaller sizes had the greatest impact on α-helicity and activity. CYST-capped QDs with an average number of the binding site ( n ) = 1, reduced α-helicity by 16% and activity by 22–30% at 7 nM concentration. In contrast, MPA-capped QDs with n  &lt; 1 had the least effect on α-helical structure and activity. The smaller GSH-capped QDs increased the activity by 9%, via partially restoring JBU’s α-helical content. The study thus thoroughly analyzed the impact of varied-size and surface-functionalized QDs on the structure and function of JBU, which can be exploited further for several biomedical applications. Graphical Abstract</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>36757588</pmid><doi>10.1007/s11356-023-25356-3</doi><tpages>23</tpages><orcidid>https://orcid.org/0000-0003-4922-9028</orcidid></addata></record>
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ispartof Environmental science and pollution research international, 2023-04, Vol.30 (16), p.48300-48322
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source MEDLINE; SpringerLink Journals
subjects Acetylcysteine
Ammonia
Aquatic Pollution
Atmospheric Protection/Air Quality Control/Air Pollution
Atomic force microscopy
Beans
Binding sites
Biomedical materials
Biomolecules
Cadmium Compounds - chemistry
Canavalia ensiformis
Carbon dioxide
Circular dichroism
circular dichroism spectroscopy
Cysteamine
Cysteine
Cysts
Dichroism
Drug delivery
drugs
Earth and Environmental Science
Ecotoxicology
Environment
Environmental Chemistry
Environmental Health
Environmental science
Excitons
Fluorescence
Glutathione
Helicity
Humans
hydrolysis
Hydrophobicity
Impact analysis
Jack beans
Microenvironments
Molecular interactions
Molecular structure
Optical properties
Photovoltaic cells
Protein structure
Quantum dots
Quantum Dots - chemistry
Research Article
Secondary structure
Selenium Compounds - chemistry
Solar cells
Spectroscopy
Structure-function relationships
Surface properties
Thermodynamics
Tumor Microenvironment
Urea
Urease
Urease - metabolism
Waste Water Technology
Water Management
Water Pollution Control
title Size- and surface functionalization-driven molecular interaction of CdSe quantum dots with jack bean urease: multispectroscopic, thermodynamic, and AFM approach
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