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  1. Article ; Online: Exploiting gold nanoparticles for diagnosis and cancer treatments.

    D'Acunto, Mario / Cioni, Patrizia / Gabellieri, Edi / Presciuttini, Gianluca

    Nanotechnology

    2021  Volume 32, Issue 19, Page(s) 192001

    Abstract: Gold nanoparticles (AuNPs) represent a relatively simple nanosystem to be synthesised and functionalized. AuNPs offer numerous advantages over different nanomaterials, primarily due to highly optimized protocols for their production with sizes in the ... ...

    Abstract Gold nanoparticles (AuNPs) represent a relatively simple nanosystem to be synthesised and functionalized. AuNPs offer numerous advantages over different nanomaterials, primarily due to highly optimized protocols for their production with sizes in the range 1-150 nm and shapes, spherical, nanorods (AuNRs), nanocages, nanostars or nanoshells (AuNSs), just to name a few. AuNPs possess unique properties both from the optical and chemical point of view. AuNPs can absorb and scatter light with remarkable efficiency. Their outstanding interaction with light is due to the conduction electrons on the metal surface undergoing a collective oscillation when they are excited by light at specific wavelengths. This oscillation, known as a localized surface plasmon resonance, causes the absorption and scattering intensities of AuNPs to be significantly higher than identically sized non-plasmonic nanoparticles. In addition, AuNP absorption and scattering properties can be tuned by controlling the particle size, shape, and the local refractive index near the particle surface. By the chemical side, AuNPs offer the advantage of functionalization with therapeutic agents through covalent and ionic binding, which can be useful for biomedical applications, with particular emphasis on cancer treatments. Functionalized AuNPs exhibit good biocompatibility and controllable distribution patterns when delivered in cells and tissues, which make them particularly fine candidates for the basis of innovative therapies. Currently, major available AuNP-based cancer therapeutic approaches are the photothermal therapy (PTT) or photodynamic therapy (PDT). PTT and PDT rely upon irradiation of surface plasmon resonant AuNPs (previously delivered in cancer cells) by light, in particular, in the near-infrared range. Under irradiation, AuNPs surface electrons are excited and resonate intensely, and fast conversion of light into heat takes place in about 1 ps. The cancer cells are destroyed by the induced hyperthermia, i.e. the condition under which cells are subject to temperature in the range of 41 °C-47 °C for tens of minutes. The review is focused on the description of the optical and thermal properties of AuNPs that underlie their continuous and progressive exploitation for diagnosis and cancer therapy.
    MeSH term(s) Animals ; Cell Line, Tumor ; Cells, Cultured ; Gold ; Humans ; Metal Nanoparticles ; Mice ; Neoplasms/diagnosis ; Neoplasms/therapy ; Particle Size ; Phototherapy ; Surface Plasmon Resonance ; Theranostic Nanomedicine
    Chemical Substances Gold (7440-57-5)
    Language English
    Publishing date 2021-01-29
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1362365-5
    ISSN 1361-6528 ; 0957-4484
    ISSN (online) 1361-6528
    ISSN 0957-4484
    DOI 10.1088/1361-6528/abe1ed
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Heat and cold denaturation of yeast frataxin: The effect of pressure.

    Puglisi, Rita / Cioni, Patrizia / Gabellieri, Edi / Presciuttini, Gianluca / Pastore, Annalisa / Temussi, Piero Andrea

    Biophysical journal

    2022  Volume 121, Issue 8, Page(s) 1502–1511

    Abstract: Yfh1 is a yeast protein with the peculiar characteristic to undergo, in the absence of salt, cold denaturation at temperatures above the water freezing point. This feature makes the protein particularly interesting for studies aiming at understanding the ...

    Abstract Yfh1 is a yeast protein with the peculiar characteristic to undergo, in the absence of salt, cold denaturation at temperatures above the water freezing point. This feature makes the protein particularly interesting for studies aiming at understanding the rules that determine protein fold stability. Here, we present the phase diagram of Yfh1 unfolding as a function of pressure (0.1-500 MPa) and temperature 278-313 K (5-40°C) both in the absence and in the presence of stabilizers using Trp fluorescence as a monitor. The protein showed a remarkable sensitivity to pressure: at 293 K, pressures around 10 MPa are sufficient to cause 50% of unfolding. Higher pressures were required for the unfolding of the protein in the presence of stabilizers. The phase diagram on the pressure-temperature plane together with a critical comparison between our results and those found in the literature allowed us to draw conclusions on the mechanism of the unfolding process under different environmental conditions.
    MeSH term(s) Cold Temperature ; Hot Temperature ; Iron-Binding Proteins ; Protein Denaturation ; Protein Folding ; Saccharomyces cerevisiae ; Thermodynamics ; Frataxin
    Chemical Substances Iron-Binding Proteins
    Language English
    Publishing date 2022-03-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2022.03.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Conjugation to gold nanoparticles of methionine gamma-lyase, a cancer-starving enzyme. Physicochemical characterization of the nanocomplex for prospective nanomedicine applications.

    Raboni, Samanta / Fumagalli, Francesco / Ceccone, Giacomo / La Spina, Rita / Ponti, Jessica / Mehn, Dora / Guerrini, Giuditta / Bettati, Stefano / Mozzarelli, Andrea / D'Acunto, Mario / Presciuttini, Gianluca / Cristallini, Caterina / Gabellieri, Edi / Cioni, Patrizia

    International journal of pharmaceutics

    2024  Volume 653, Page(s) 123882

    Abstract: The pyridoxal 5'-dependent enzyme methionine γ-lyase (MGL) catalyzes the degradation of methionine. This activity has been profitable to develop an antitumor agent exploiting the strict dependence of most malignant cells on the availability of methionine. ...

    Abstract The pyridoxal 5'-dependent enzyme methionine γ-lyase (MGL) catalyzes the degradation of methionine. This activity has been profitable to develop an antitumor agent exploiting the strict dependence of most malignant cells on the availability of methionine. Indeed, methionine depletion blocks tumor proliferation and leads to an increased susceptibility to anticancer drugs. Here, we explore the conjugation of MGL to gold nanoparticles capped with citrate (AuNPs) as a novel strategy to deliver MGL to cancer cells. Measurements of Transmission Electron Microscopy, Dynamic Light Scattering, Asymmetrical Flow Field-Flow Fractionation, X-ray Photoelectron Spectroscopy, and Circular Dichroism allowed to achieve an extensive biophysical and biochemical characterization of the MGL-AuNP complex including particle size, size distribution, MGL loading yield, enzymatic activity, and impact of gold surface on protein structure. Noticeably, we found that activity retention was improved over time for the enzyme adsorbed to AuNPs with respect to the enzyme free in solution. The acquired body of knowledge on the nanocomplex properties and this encouraging stabilizing effect upon conjugation are the necessary basis for further studies aimed at the evaluation of the therapeutic potential of MGL-AuNP complex in a biological milieu.
    MeSH term(s) Humans ; Gold/chemistry ; Nanomedicine ; Prospective Studies ; Metal Nanoparticles/chemistry ; Neoplasms/drug therapy ; Neoplasms/pathology ; Antineoplastic Agents/chemistry ; Methionine ; Carbon-Sulfur Lyases
    Chemical Substances Gold (7440-57-5) ; L-methionine gamma-lyase (EC 4.4.1.11) ; Antineoplastic Agents ; Methionine (AE28F7PNPL) ; Carbon-Sulfur Lyases (EC 4.4.-)
    Language English
    Publishing date 2024-02-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 428962-6
    ISSN 1873-3476 ; 0378-5173
    ISSN (online) 1873-3476
    ISSN 0378-5173
    DOI 10.1016/j.ijpharm.2024.123882
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A Copper nanoparticles-based polymeric spray coating: Nanoshield against Sars-Cov-2.

    Foffa, Ilenia / Losi, Paola / Quaranta, Paola / Cara, Alice / Al Kayal, Tamer / D'Acunto, Mario / Presciuttini, Gianluca / Pistello, Mauro / Soldani, Giorgio

    Journal of applied biomaterials & functional materials

    2022  Volume 20, Page(s) 22808000221076326

    Abstract: Face masks are an effective protection tool to prevent bacterial and viral transmission. However, commercial face masks contain filters made of materials that are not capable of inactivating either SARS-CoV-2. In this regard, we report the development of ...

    Abstract Face masks are an effective protection tool to prevent bacterial and viral transmission. However, commercial face masks contain filters made of materials that are not capable of inactivating either SARS-CoV-2. In this regard, we report the development of an antiviral coating of polyurethane and Copper nanoparticles on a face mask filter fabricated with a spray technology that is capable of inactivating more than 99% of SARS-CoV-2 particles in 30 min of contact.
    MeSH term(s) COVID-19/prevention & control ; Copper ; Humans ; Masks ; Nanoparticles ; Polymers ; SARS-CoV-2
    Chemical Substances Polymers ; Copper (789U1901C5)
    Language English
    Publishing date 2022-05-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2673624-X
    ISSN 2280-8000 ; 2280-8000
    ISSN (online) 2280-8000
    ISSN 2280-8000
    DOI 10.1177/22808000221076326
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: A novel hotspot of gelsolin instability triggers an alternative mechanism of amyloid aggregation

    Bollati, Michela / Diomede, Luisa / Giorgino, Toni / Natale, Carmina / Fagnani, Elisa / Boniardi, Irene / Barbiroli, Alberto / Alemani, Rebecca / Beeg, Marten / Gobbi, Marco / Fakin, Ana / Mastrangelo, Eloise / Milani, Mario / Presciuttini, Gianluca / Gabellieri, Edi / Cioni, Patrizia / de Rosa, Matteo

    Computational and Structural Biotechnology Journal. 2021, v. 19

    2021  

    Abstract: Gelsolin comprises six homologous domains, named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease causing progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Although ... ...

    Abstract Gelsolin comprises six homologous domains, named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease causing progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Although several different amyloidogenic variants of gelsolin have been identified, only the most common mutants present in the G2 domain have been thoroughly characterized, leading to clarification of the functional mechanism. The molecular events underlying the pathological aggregation of 3 recently identified mutations, namely A551P, E553K and M517R, all localized at the interface between G4 and G5, are here explored for the first time. Structural studies point to destabilization of the interface between G4 and G5 due to three structural determinants: β-strand breaking, steric hindrance and/or charge repulsion, all implying impairment of interdomain contacts. Such rearrangements decrease the temperature and pressure stability of gelsolin but do not alter its susceptibility to furin cleavage, the first event in the canonical aggregation pathway. These variants also have a greater tendency to aggregate in the unproteolysed forms and exhibit higher proteotoxicity in a C. elegans-based assay. Our data suggest that aggregation of G4G5 variants follows an alternative, likely proteolysis-independent, pathway.
    Keywords amyloid ; amyloidosis ; biotechnology ; cornea ; temperature
    Language English
    Size p. 6355-6365.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 2694435-2
    ISSN 2001-0370
    ISSN 2001-0370
    DOI 10.1016/j.csbj.2021.11.025
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: A novel hotspot of gelsolin instability triggers an alternative mechanism of amyloid aggregation.

    Bollati, Michela / Diomede, Luisa / Giorgino, Toni / Natale, Carmina / Fagnani, Elisa / Boniardi, Irene / Barbiroli, Alberto / Alemani, Rebecca / Beeg, Marten / Gobbi, Marco / Fakin, Ana / Mastrangelo, Eloise / Milani, Mario / Presciuttini, Gianluca / Gabellieri, Edi / Cioni, Patrizia / de Rosa, Matteo

    Computational and structural biotechnology journal

    2021  Volume 19, Page(s) 6355–6365

    Abstract: Gelsolin comprises six homologous domains, named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease causing progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Although ... ...

    Abstract Gelsolin comprises six homologous domains, named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease causing progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Although several different amyloidogenic variants of gelsolin have been identified, only the most common mutants present in the G2 domain have been thoroughly characterized, leading to clarification of the functional mechanism. The molecular events underlying the pathological aggregation of 3 recently identified mutations, namely A551P, E553K and M517R, all localized at the interface between G4 and G5, are here explored for the first time. Structural studies point to destabilization of the interface between G4 and G5 due to three structural determinants: β-strand breaking, steric hindrance and/or charge repulsion, all implying impairment of interdomain contacts. Such rearrangements decrease the temperature and pressure stability of gelsolin but do not alter its susceptibility to furin cleavage, the first event in the canonical aggregation pathway. These variants also have a greater tendency to aggregate in the unproteolysed forms and exhibit higher proteotoxicity in a
    Language English
    Publishing date 2021-11-19
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2694435-2
    ISSN 2001-0370
    ISSN 2001-0370
    DOI 10.1016/j.csbj.2021.11.025
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: A SELDI-TOF approach to ecotoxicology: comparative profiling of low molecular weight proteins from a marine diatom exposed to CdSe/ZnS quantum dots.

    Scebba, Francesca / Tognotti, Danika / Presciuttini, Gianluca / Gabellieri, Edi / Cioni, Patrizia / Angeloni, Debora / Basso, Barbara / Morelli, Elisabetta

    Ecotoxicology and environmental safety

    2016  Volume 123, Page(s) 45–52

    Abstract: Quantum dots (QDs), namely semiconductor nanocrystals, due to their particular optical and electronic properties, have growing applications in device technology, biotechnology and biomedical fields. Nevertheless, the possible threat to human health and ... ...

    Abstract Quantum dots (QDs), namely semiconductor nanocrystals, due to their particular optical and electronic properties, have growing applications in device technology, biotechnology and biomedical fields. Nevertheless, the possible threat to human health and the environment have attracted increasing attention as the production and applications of QDs increases rapidly while standard evaluation of safety lags. In the present study we performed proteomic analyses, by means of 2D gel electrophoresis and Surface Enhanced Laser Desorption Ionization-Time of Flight-Mass Spectrometry (SELDI-TOF-MS). We aimed to identify potential biomarkers of exposure to CdSe/ZnS quantum dots. The marine diatom Phaeodactylum tricornutum exposed to 2.5nM QDs was used as a model system. Both 2DE and SELDI showed the presence of differentially expressed proteins. By Principal Component Analysis (PCA) we were able to show that the differentially expressed proteins can discriminate between exposed and not exposed cells. Furthermore, a protein profile specific for exposed cells was obtained by SELDI analysis. To our knowledge, this is the first example of the application of SELDI technology to the analysis of microorganisms used as biological sentinel model of marine environmental pollution.
    MeSH term(s) Cadmium Compounds/toxicity ; Diatoms/drug effects ; Diatoms/growth & development ; Ecotoxicology ; Gene Expression ; Models, Biological ; Molecular Weight ; Principal Component Analysis ; Proteome/analysis ; Proteomics ; Quantum Dots/toxicity ; Selenium Compounds/toxicity ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Sulfides/toxicity ; Zinc Compounds/toxicity
    Chemical Substances Cadmium Compounds ; Proteome ; Selenium Compounds ; Sulfides ; Zinc Compounds ; cadmium selenide (A7F646JC5C) ; zinc sulfide (KPS085631O)
    Language English
    Publishing date 2016-01
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 436536-7
    ISSN 1090-2414 ; 0147-6513
    ISSN (online) 1090-2414
    ISSN 0147-6513
    DOI 10.1016/j.ecoenv.2015.08.024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book ; Online: A novel hotspot of gelsolin instability and aggregation propensity triggers a new mechanism of amyloidosis

    Bollati, Michela / Diomede, Luisa / Giorgino, Toni / Natale, Carmina / Fagnani, Elisa / Boniardi, Irene / Barbiroli, Alberto / Alemani, Rebecca / Beeg, Marten / Gobbi, Marco / Fakin, Ana / Mastrangelo, Eloise / Milani, Mario / Presciuttini, Gianluca / Gabellieri, Edi / Cioni, Patrizia / de Rosa, Matteo

    2021  

    Abstract: The multidomain protein gelsolin (GSN) is composed of six homologous modules, sequentially named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease characterized by progressive corneal lattice ... ...

    Abstract The multidomain protein gelsolin (GSN) is composed of six homologous modules, sequentially named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease characterized by progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Several different amyloidogenic variants of GSN have been identified over the years, but only the most common D187N/Y mutants, in G2, have been thoroughly characterized, and the underlying functional mechanistic link between mutation, altered protein structure, susceptibility to aberrant furin cleavage and aggregative potential resolved. Little is known about the recently identified mutations A551P, E553K and M517R hosted at the interface between G4 and G5, whose aggregation process likely follows an alternative pathway. We demonstrate that these three substitutions impair temperature and pressure stability of GSN but do not increase its susceptibility to furin cleavage, the first event of the canonical aggregation pathway. The variants are also characterized by a higher tendency to aggregate in the unproteolysed forms and show a higher proteotoxicity in a C. elegans-based assay. Structural studies point to a destabilization of the interface between G4 and G5 due to three different structural determinants: beta-strand breaking, steric hindrance and/or charge repulsion, all implying the impairment of interdomain contacts. All available evidence suggests that the rearrangement of the protein global architecture triggers a furin-independent aggregation of the protein, supporting the existence of a non-canonical pathway of gelsolin amyloidosis pathogenesis.

    Comment: main: 28 pages, 7 figures; supplementary: 11 pages, 6 figures
    Keywords Quantitative Biology - Biomolecules
    Subject code 570
    Publishing date 2021-09-15
    Publishing country us
    Document type Book ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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