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  1. Article ; Online: Correction to "On-Chip Sample Preparation Using a ChipFilter Coupled to NanoLC-MS/MS for Bottom-Up Proteomics".

    Ndiaye, Massamba M / Ta, Ha Phuong / Chiappetta, Giovanni / Vinh, Joëlle

    Journal of proteome research

    2021  Volume 20, Issue 12, Page(s) 5424

    Language English
    Publishing date 2021-11-03
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.1c00846
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6189: Show issues Location:
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  2. Article ; Online: Effect of Graphene Oxide on Liquid Water-Based Waterproofing Bituminous Membranes.

    Di Luca, Giuseppe / Filomia, Marcello / Fuoco, Alessio / Chiappetta, Giovanni / Figoli, Alberto

    Polymers

    2022  Volume 14, Issue 11

    Abstract: In this work, innovative graphene oxide-doped waterproofing bituminous membranes, also called roof bituminous membranes, were prepared and characterized in terms of physicochemical and vapor transport properties. The results showed that the introduction ... ...

    Abstract In this work, innovative graphene oxide-doped waterproofing bituminous membranes, also called roof bituminous membranes, were prepared and characterized in terms of physicochemical and vapor transport properties. The results showed that the introduction of a small amount of GO increased the mechanical resistance of the doped membranes compared to the native one. Moreover, the addition of the GO leads to a remarkable chemical stability of the membranes when exposed to UV radiation and high temperatures. Furthermore, a decrease in water vapor permeation was observed when GO was present in the membrane matrix compared to native bituminous membranes, demonstrating that an addition of GO can boost the waterproofing properties of these bituminous membranes.
    Language English
    Publishing date 2022-05-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527146-5
    ISSN 2073-4360 ; 2073-4360
    ISSN (online) 2073-4360
    ISSN 2073-4360
    DOI 10.3390/polym14112221
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  3. Article: Effect of the Post-Spinning Solvent Exchange on the Performance of Asymmetric, Polyimide Hollow Fibers Prepared by Using a Triple-Orifice Spinneret.

    Bernardo, Paola / Tasselli, Franco / Chiappetta, Giovanni / Clarizia, Gabriele

    Materials (Basel, Switzerland)

    2019  Volume 12, Issue 21

    Abstract: Hollow fibers (HFs) are widely applied in different membrane operations, particularly in gas separation. The present work investigates the effect of post-spinning treatment on the gas transport properties of polyimide-based HFs. The membranes were spun ... ...

    Abstract Hollow fibers (HFs) are widely applied in different membrane operations, particularly in gas separation. The present work investigates the effect of post-spinning treatment on the gas transport properties of polyimide-based HFs. The membranes were spun by using both a conventional spinneret and a triple-orifice spinneret. A systematic analysis was carried out by considering different alcohols as the first fluid for the solvent exchange, with or without
    Language English
    Publishing date 2019-11-05
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2487261-1
    ISSN 1996-1944
    ISSN 1996-1944
    DOI 10.3390/ma12213632
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  4. Article ; Online: Study of metalation of thioredoxin by gold(I) therapeutic compounds using combined liquid chromatography/capillary electrophoresis with inductively coupled plasma/electrospray MS/MS detection.

    Bernabeu De Maria, Mikel / Matczuk, Magdalena / Tesauro, Diego / Saviano, Michele / Sikorski, Jacek / Chiappetta, Giovanni / Godin, Simon / Szpunar, Joanna / Lobinski, Ryszard / Ronga, Luisa

    Analytical and bioanalytical chemistry

    2024  Volume 416, Issue 11, Page(s) 2819–2833

    Abstract: The reactivity of thioredoxin (Trx1) with the Au(I) drug auranofin (AF) and two therapeutic N-heterocyclic carbene (NHC) ...

    Abstract The reactivity of thioredoxin (Trx1) with the Au(I) drug auranofin (AF) and two therapeutic N-heterocyclic carbene (NHC)
    MeSH term(s) Gold/chemistry ; Tandem Mass Spectrometry ; Auranofin ; Spectrometry, Mass, Electrospray Ionization ; Gold Compounds/chemistry ; Electrophoresis, Capillary ; Immunologic Factors ; Chromatography, Liquid ; Thioredoxins
    Chemical Substances Gold (7440-57-5) ; Auranofin (3H04W2810V) ; Gold Compounds ; Immunologic Factors ; Thioredoxins (52500-60-4)
    Language English
    Publishing date 2024-01-20
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 201093-8
    ISSN 1618-2650 ; 0016-1152 ; 0372-7920
    ISSN (online) 1618-2650
    ISSN 0016-1152 ; 0372-7920
    DOI 10.1007/s00216-024-05140-z
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    In stock of ZB MED Bonn / Germany

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  5. Article ; Online: On-Chip Sample Preparation Using a ChipFilter Coupled to NanoLC-MS/MS for Bottom-Up Proteomics.

    Ndiaye, Massamba M / Ta, Ha Phuong / Chiappetta, Giovanni / Vinh, Joëlle

    Journal of proteome research

    2020  Volume 19, Issue 7, Page(s) 2654–2663

    Abstract: Sample preparation is a crucial step in bottom-up proteomics. Analytical performances of bottom-up proteomics can be improved by the miniaturization of sample preparation. Many microfluidic devices have been designed in the field of proteomics, but many ... ...

    Abstract Sample preparation is a crucial step in bottom-up proteomics. Analytical performances of bottom-up proteomics can be improved by the miniaturization of sample preparation. Many microfluidic devices have been designed in the field of proteomics, but many of them are not capable of handling complex samples and do not integrate the processing and digestion steps. We propose a ChipFilter Proteolysis (CFP) microfluidic device as a proteomics reactor for the miniaturization of protein sample processing and digestion steps, whose design is closely related to the experimental setup of filter-aided sample processing, even if no denaturing surfactant is required. The microchip has two reaction chambers of 0.6 μL volume separated by a protein filtration membrane in regenerated cellulose (10kD cutoff) that will concentrate or retain large polypeptides and will release small molecules. Cell lysis, protein concentration, and rapid chemical or enzymatic treatment can be performed in the ChipFilter. Complex proteomic samples like yeast protein extract or whole human cells proteome have been successfully analyzed with our microchip. Compared with the membrane-based commercial ultracentrifugation cartridge, our microfluidic device offered a better proteome coverage with 10 times less starting material and 8 times faster protocol duration.
    MeSH term(s) Humans ; Proteolysis ; Proteome ; Proteomics ; Specimen Handling ; Tandem Mass Spectrometry
    Chemical Substances Proteome
    Language English
    Publishing date 2020-05-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.9b00832
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6189: Show issues Location:
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  6. Article: Potential of Fourier Transform Mass Spectrometry (Orbitrap and Ion Cyclotron Resonance) for Speciation of the Selenium Metabolome in Selenium-Rich Yeast.

    Bierla, Katarzyna / Chiappetta, Giovanni / Vinh, Joëlle / Lobinski, Ryszard / Szpunar, Joanna

    Frontiers in chemistry

    2020  Volume 8, Page(s) 612387

    Abstract: The evolution of the field of element speciation, from the targeted analysis for specific element species toward a global exploratory analysis for the entirety of metal- or metalloid-related compounds present in a biological system (metallomics), ... ...

    Abstract The evolution of the field of element speciation, from the targeted analysis for specific element species toward a global exploratory analysis for the entirety of metal- or metalloid-related compounds present in a biological system (metallomics), requires instrumental techniques with increasing selectivity and sensitivity. The selectivity of hyphenated techniques, combining chromatography, and capillary electrophoresis with element-specific detection (usually inductively coupled plasma mass spectrometry, ICP MS), is often insufficient to discriminate all the species of a given element in a sample. The necessary degree of specificity can be attained by ultrahigh-resolution (R >100,000 in the
    Language English
    Publishing date 2020-12-09
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2020.612387
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  7. Article ; Online: Lifestyle-specific S-nitrosylation of protein cysteine thiols regulates Escherichia coli biofilm formation and resistance to oxidative stress.

    Barraud, Nicolas / Létoffé, Sylvie / Beloin, Christophe / Vinh, Joelle / Chiappetta, Giovanni / Ghigo, Jean-Marc

    NPJ biofilms and microbiomes

    2021  Volume 7, Issue 1, Page(s) 34

    Abstract: Communities of bacteria called biofilms are characterized by reduced diffusion, steep oxygen, and redox gradients and specific properties compared to individualized planktonic bacteria. In this study, we investigated whether signaling via nitrosylation ... ...

    Abstract Communities of bacteria called biofilms are characterized by reduced diffusion, steep oxygen, and redox gradients and specific properties compared to individualized planktonic bacteria. In this study, we investigated whether signaling via nitrosylation of protein cysteine thiols (S-nitrosylation), regulating a wide range of functions in eukaryotes, could also specifically occur in biofilms and contribute to bacterial adaptation to this widespread lifestyle. We used a redox proteomic approach to compare cysteine S-nitrosylation in aerobic and anaerobic biofilm and planktonic Escherichia coli cultures and we identified proteins with biofilm-specific S-nitrosylation status. Using bacterial genetics and various phenotypic screens, we showed that impairing S-nitrosylation in proteins involved in redox homeostasis and amino acid synthesis such as OxyR, KatG, and GltD altered important biofilm properties, including motility, biofilm maturation, or resistance to oxidative stress. Our study therefore revealed that S-nitrosylation constitutes a physiological basis underlying functions critical for E. coli adaptation to the biofilm environment.
    MeSH term(s) Amino Acids/metabolism ; Biofilms/growth & development ; Cysteine/metabolism ; Escherichia coli/physiology ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Homeostasis ; Mutation ; Oxidation-Reduction ; Oxidative Stress ; Phenotype ; Protein Processing, Post-Translational ; Proteome ; Proteomics/methods ; Sulfhydryl Compounds/metabolism
    Chemical Substances Amino Acids ; Escherichia coli Proteins ; Proteome ; Sulfhydryl Compounds ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2021-04-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2817021-0
    ISSN 2055-5008 ; 2055-5008
    ISSN (online) 2055-5008
    ISSN 2055-5008
    DOI 10.1038/s41522-021-00203-w
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  8. Article ; Online: Upgrade of an old drug: Auranofin in innovative cancer therapies to overcome drug resistance and to increase drug effectiveness.

    Gamberi, Tania / Chiappetta, Giovanni / Fiaschi, Tania / Modesti, Alessandra / Sorbi, Flavia / Magherini, Francesca

    Medicinal research reviews

    2021  Volume 42, Issue 3, Page(s) 1111–1146

    Abstract: Auranofin is an oral gold(I) compound, initially developed for the treatment of rheumatoid arthritis. Currently, Auranofin is under investigation for oncological application within a drug repurposing plan due to the relevant antineoplastic activity ... ...

    Abstract Auranofin is an oral gold(I) compound, initially developed for the treatment of rheumatoid arthritis. Currently, Auranofin is under investigation for oncological application within a drug repurposing plan due to the relevant antineoplastic activity observed both in vitro and in vivo tumor models. In this review, we analysed studies in which Auranofin was used as a single drug or in combination with other molecules to enhance their anticancer activity or to overcome chemoresistance. The analysis of different targets/pathways affected by this drug in different cancer types has allowed us to highlight several interesting targets and effects of Auranofin besides the already well-known inhibition of thioredoxin reductase. Among these targets, inhibitory-κB kinase, deubiquitinates, protein kinase C iota have been frequently suggested. To rationalize the effects of Auranofin by a system biology-like approach, we exploited transcriptomic data obtained from a wide range of cell models, extrapolating the data deposited in the Connectivity Maps website and we attempted to provide a general conclusion and discussed the major points that need further investigation.
    MeSH term(s) Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Auranofin/pharmacology ; Auranofin/therapeutic use ; Drug Resistance ; Humans ; Neoplasms/drug therapy ; Neoplasms/pathology ; Thioredoxin-Disulfide Reductase
    Chemical Substances Antineoplastic Agents ; Auranofin (3H04W2810V) ; Thioredoxin-Disulfide Reductase (EC 1.8.1.9)
    Language English
    Publishing date 2021-12-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 603210-2
    ISSN 1098-1128 ; 0198-6325
    ISSN (online) 1098-1128
    ISSN 0198-6325
    DOI 10.1002/med.21872
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    Zs.A 1764: Show issues Location:
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  9. Article ; Online: Redox proteome analysis of auranofin exposed ovarian cancer cells (A2780).

    Chiappetta, Giovanni / Gamberi, Tania / Faienza, Fiorella / Limaj, Xhesika / Rizza, Salvatore / Messori, Luigi / Filomeni, Giuseppe / Modesti, Alessandra / Vinh, Joelle

    Redox biology

    2022  Volume 52, Page(s) 102294

    Abstract: The effects of Auranofin (AF) on protein expression and protein oxidation in A2780 cancer cells were investigated through a strategy based on simultaneous expression proteomics and redox proteomics determinations. Bioinformatics analysis of the ... ...

    Abstract The effects of Auranofin (AF) on protein expression and protein oxidation in A2780 cancer cells were investigated through a strategy based on simultaneous expression proteomics and redox proteomics determinations. Bioinformatics analysis of the proteomics data supports the view that the most critical cellular changes elicited by AF treatment consist of thioredoxin reductase inhibition, alteration of the cell redox state, impairment of the mitochondrial functions, metabolic changes associated with conversion to a glycolytic phenotype, induction of ER stress. The occurrence of the above cellular changes was extensively validated by performing direct biochemical assays. Our data are consistent with the concept that AF produces its effects through a multitarget mechanism that mainly affects the redox metabolism and the mitochondrial functions and results into severe ER stress. Results are discussed in the context of the current mechanistic knowledge existing on AF.
    MeSH term(s) Auranofin/pharmacology ; Cell Line, Tumor ; Female ; Humans ; Ovarian Neoplasms/drug therapy ; Ovarian Neoplasms/genetics ; Oxidation-Reduction ; Proteome/metabolism ; Thioredoxin-Disulfide Reductase/metabolism
    Chemical Substances Proteome ; Auranofin (3H04W2810V) ; Thioredoxin-Disulfide Reductase (EC 1.8.1.9)
    Language English
    Publishing date 2022-03-22
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701011-9
    ISSN 2213-2317 ; 2213-2317
    ISSN (online) 2213-2317
    ISSN 2213-2317
    DOI 10.1016/j.redox.2022.102294
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  10. Article ; Online: Investigation of serum proteome homeostasis during radiation therapy by a quantitative proteomics approach.

    Ouerhani, Amira / Chiappetta, Giovanni / Souiai, Oussema / Mahjoubi, Halima / Vinh, Joelle

    Bioscience reports

    2019  Volume 39, Issue 7

    Abstract: The purpose of the present study is to analyze the serum proteome of patients receiving Radiation Therapy (RT) at different stages of their treatment to discovery candidate biomarkers of the radiation-induced skin lesions and the molecular pathways ... ...

    Abstract The purpose of the present study is to analyze the serum proteome of patients receiving Radiation Therapy (RT) at different stages of their treatment to discovery candidate biomarkers of the radiation-induced skin lesions and the molecular pathways underlying the radiation signatures. Six stages of RT treatment were monitored from patients treated because of brain cancer: before starting the treatment, during the treatment (four time points), and at 4 weeks from the last RT dose. Serum samples were analyzed by a proteomics approach based on the Data Independent Acquisition (DIA) mass spectrometry (MS). RT induced clear changes in the expression levels of 36 serum proteins. Among these, 25 proteins were down- or up-regulated significantly before the emergence of skin lesions. Some of these were still deregulated after the completion of the treatment. Few days before the appearance of the skin lesions, the levels of some proteins involved in the wound healing processes were down-regulated. The pathway analysis indicated that after partial body irradiation, the expression levels of proteins functionally involved in the acute inflammatory and immune response, lipoprotein process and blood coagulation, were deregulated.
    MeSH term(s) Adult ; Blood Proteins/metabolism ; Female ; Humans ; Male ; Middle Aged ; Proteome/metabolism ; Proteomics ; Radiation Injuries/blood ; Radiotherapy/adverse effects
    Chemical Substances Blood Proteins ; Proteome
    Language English
    Publishing date 2019-07-29
    Publishing country England
    Document type Clinical Trial ; Journal Article
    ZDB-ID 764946-0
    ISSN 1573-4935 ; 0144-8463
    ISSN (online) 1573-4935
    ISSN 0144-8463
    DOI 10.1042/BSR20182319
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