Interaction of silver nanoparticles with plasma transport proteins: A systematic study on impacts of particle size, shape and surface functionalization

Barbir, Rinea; Capjak, Ivona; Crnković, Tea; Debeljak, Željko; Jurašin, Darija Domazet; Ćurlin, Marija; Šinko, Goran; Weitner, Tin; Vrček, Ivana Vinković

doi:10.1016/j.cbi.2020.109364

Cited by 13 publications

(10 citation statements)

References 65 publications

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“…On the contrary, as the size of CIT-coated AuNPs increased, binding affinities with TRF and ngTRF were stronger (Table S2 in the Supporting Information). Also, binding affinities for BSA decreased with the increase in size of PVP-coated AgNPs, which is in good agreement with previously published research, but an opposite trend was observed for interaction of this AgNM type with TRF and ngTRF. Nevertheless, spherical NMs showed a completely opposite trend for the protein binding with the size change for Au compared to Ag core.…”

Section: Resultssupporting

confidence: 92%

“…In addition to TRF and ngTRF, bovine serum albumin (BSA) was included for comparative purposes due to a large number of scientific data on nano-biointeractions with this protein. Our recent study compared interaction between different AgNMs with BSA and α-1-acid glycoprotein, as representatives of nonglycosylated vs glycosylated human serum proteins, respectively . However, these two proteins differ not only in glycosylation status but also in their secondary structure and conformation.…”

Section: Introductionmentioning

confidence: 99%

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Interaction of Differently Sized, Shaped, and Functionalized Silver and Gold Nanoparticles with Glycosylated versus Nonglycosylated Transferrin

Barbir

Jiménez

Martín‐Rapún

et al. 2021

ACS Appl. Mater. Interfaces

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Exposure of nanomaterials (NMs) to biological medium results in their direct interaction with biomolecules and the formation of a dynamic biomolecular layer known as the biomolecular corona. Despite numerous published data on nano-biointeractions, the role of protein glycosylation in the formation, characteristics, and fate of such nano-biocomplexes has been almost completely neglected, although most serum proteins are glycosylated. This study aimed to systematically investigate the differences in interaction of metallic NPs with glycosylated vs nonglycosylated transferrin. To reach this aim, we compared interaction mechanisms between differently sized, shaped, and surface-functionalized silver NMs and gold NMs to commercially available human transferrin (TRF), a glycosylated protein, and to its nonglycosylated recombinant form (ngTRF). Bovine serum albumin (BSA) was also included in the study for comparative purposes. Characterization of NMs was performed using transmission electron microscopy and dynamic and electrophoretic light scattering techniques. Fluorescence quenching and circular dichroism methods were used to evaluate protein binding constants on the nanosurface and conformational changes after the protein–NM interactions, respectively. Competitive binding of TRF, ngTRF, and BSA to the surface of different NMs was evaluated by separating them after extraction from protein corona by gel electrophoresis following quantification with a commercial protein assay. The results showed that the binding strength between NMs and transferrin and the changes in the secondary protein structure largely depend not only on NM physicochemical properties but also on the protein glycosylation status. Data gained by this study highlight the relevance of protein glycosylation for all future design, development, and efficacy and safety assessment of NMs.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Interaction of Differently Sized, Shaped, and Functionalized Silver and Gold Nanoparticles with Glycosylated versus Nonglycosylated Transferrin

Barbir

Jiménez

Martín‐Rapún

et al. 2021

ACS Appl. Mater. Interfaces

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“…Barbir et al. ( 21 ) studied the effects of silver nanoparticles on the structure of plasma transport proteins by CD.…”

Section: Resultsmentioning

confidence: 99%

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

Micsonai

Moussong

Wien

et al. 2022

Nucleic Acids Research

158

121

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Circular dichroism (CD) spectroscopy is widely used to characterize the secondary structure composition of proteins. To derive accurate and detailed structural information from the CD spectra, we have developed the Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which can handle the spectral diversity of β-structured proteins. The BeStSel webserver provides this method with useful accessories to the community with the main goal to analyze single or multiple protein CD spectra. Uniquely, BeStSel provides information on eight secondary structure components including parallel β-structure and antiparallel β-sheets with three different groups of twist. It overperforms any available method in accuracy and information content, moreover, it is capable of predicting the protein fold down to the topology/homology level of the CATH classification. A new module of the webserver helps to distinguish intrinsically disordered proteins by their CD spectrum. Secondary structure calculation for uploaded PDB files will help the experimental verification of protein MD and in silico modelling using CD spectroscopy. The server also calculates extinction coefficients from the primary sequence for CD users to determine the accurate protein concentrations which is a prerequisite for reliable secondary structure determination. The BeStSel server can be freely accessed at https://bestsel.elte.hu.

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“…The literature reports that for any nanomaterials or nanoparticles designed for medicinal purposes, the role of coating agents or corona is very important for surface stabilization and nanoparticles effects. It is a critically important factor in designing and developing safe and efficient nanomaterials [36,37]. Reports also suggest that AgNPs may transform very quickly during their journey through different biological conditions.…”

Section: Antibacterial Activity Of P-agnps and E-agnpsmentioning

confidence: 99%

Antibacterial Effect of Silver Nanoparticles Is Stronger If the Production Host and the Targeted Pathogen Are Closely Related

Singh

Mijaković

2022

Biomedicines

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Microbial resistance to antibiotics is one of the key challenges that lead to the search for alternate antimicrobial treatment approaches. Silver nanoparticles (AgNPs) are well known for their antimicrobial effects against a wide variety of drug-resistant microorganisms. AgNPs can be synthesized using microbial hosts, using a green and economical synthesis route, which produces extremely stable and highly active nanoparticles. Such green AgNPs are coated with a biological coating often referred to as a corona, originating from the production microorganism. In this study, we asked whether the composition of the biological corona might influence the antimicrobial activity of green AgNPs. To investigate this, we produced AgNPs in Pseudomonas putida KT2440 and Escherichia coli K12 MG1655, and tested them against pathogen species from the corresponding genera. AgNPs exhibited a size range of 15–40 nm for P. putida and 30–70 nm for E. coli, and both types of nanoparticles were surrounded by a thick biological corona layer, providing extreme stability. The nanoparticles remained stable over long periods and exhibited negative zeta potential values. P-AgNPs (obtained from P. putida) were tested against pathogenic Pseudomonas aeruginosa PAO1, and E-AgNPs (obtained from E. coli) were tested against pathogenic Escherichia coli UTI 89. Antimicrobial studies were conducted by Minimum bactericidal concentration (MBC), live/dead staining and SEM analysis. MBC of P-AgNPs against P. aeruginosa was 1 μg/mL, and MBC of E-AgNPs against E. coli UTI 89 was 8 μg/mL. In both cases, the MBC values were superior to those of green AgNPs produced in organisms unrelated to the target pathogens, available in the literature. Our results suggest that NPs produced in microorganisms closely related to the target pathogen may be more effective, indicating that the composition of the biological corona may play a crucial role in the antimicrobial mechanism of AgNPs.

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Interaction of silver nanoparticles with plasma transport proteins: A systematic study on impacts of particle size, shape and surface functionalization

Cited by 13 publications

References 65 publications

Interaction of Differently Sized, Shaped, and Functionalized Silver and Gold Nanoparticles with Glycosylated versus Nonglycosylated Transferrin

Interaction of Differently Sized, Shaped, and Functionalized Silver and Gold Nanoparticles with Glycosylated versus Nonglycosylated Transferrin

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

Antibacterial Effect of Silver Nanoparticles Is Stronger If the Production Host and the Targeted Pathogen Are Closely Related

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