Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein

Giorgia Brancolini, Alessandra Corazza, Marco Vuano, Federico Fogolari, Maria Chiara Mimmi, Vittorio Bellotti, Monica Stoppini, Stefano Corni, Gennaro Esposito

    Research output: Contribution to journalArticle

    Abstract

    Nanoparticles (NPs) are known to exhibit distinct physical and chemical properties compared with the same materials in bulk form. NPs have been repeatedly reported to interact with proteins, and this interaction can be exploited to affect processes undergone by proteins, such as fibrillogenesis. Fibrillation is common to many proteins, and in living organisms, it causes tissue-specific or systemic amyloid diseases. The nature of NPs and their surface chemistry is crucial in assessing their affinity for proteins and their effects on them. Here we present the first detailed structural characterization and molecular mechanics model of the interaction between a fibrillogenic protein, β2-microglobulin, and a NP, 5 nm hydrophilic citrate-capped gold nanoparticles. NMR measurements and simulations at multiple levels (enhanced sampling molecular dynamics, Brownian dynamics, and Poisson-Boltzmann electrostatics) explain the origin of the observed protein perturbations mostly localized at the amino-terminal region. Experiments show that the protein-NP interaction is weak in the physiological-like, conditions and do not induce protein fibrillation. Simulations reproduce these findings and reveal instead the role of the citrate in destabilizing the lower pH protonated form of β2-microglobulin. The results offer possible strategies for controlling the desired effect of NPs on the conformational changes of the proteins, which have significant roles in the fibrillation process.

    Original languageEnglish (US)
    Pages (from-to)2600-2613
    Number of pages14
    JournalACS Nano
    Volume9
    Issue number3
    DOIs
    StatePublished - Jan 1 2015

    Fingerprint

    Amyloidogenic Proteins
    citrates
    Citric Acid
    Gold
    gold
    Nanoparticles
    proteins
    Proteins
    nanoparticles
    fibrillation
    Molecular mechanics
    Surface chemistry
    organisms
    Amyloid
    chemical properties
    Chemical properties
    affinity
    Molecular dynamics
    Electrostatics
    simulation

    Keywords

    • amyloid
    • docking
    • fibrillogenesis
    • molecular dynamics
    • nanoparticles
    • nuclear magnetic resonance

    ASJC Scopus subject areas

    • Materials Science(all)
    • Engineering(all)
    • Physics and Astronomy(all)

    Cite this

    Brancolini, G., Corazza, A., Vuano, M., Fogolari, F., Mimmi, M. C., Bellotti, V., ... Esposito, G. (2015). Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein. ACS Nano, 9(3), 2600-2613. https://doi.org/10.1021/nn506161j

    Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein. / Brancolini, Giorgia; Corazza, Alessandra; Vuano, Marco; Fogolari, Federico; Mimmi, Maria Chiara; Bellotti, Vittorio; Stoppini, Monica; Corni, Stefano; Esposito, Gennaro.

    In: ACS Nano, Vol. 9, No. 3, 01.01.2015, p. 2600-2613.

    Research output: Contribution to journalArticle

    Brancolini, G, Corazza, A, Vuano, M, Fogolari, F, Mimmi, MC, Bellotti, V, Stoppini, M, Corni, S & Esposito, G 2015, 'Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein', ACS Nano, vol. 9, no. 3, pp. 2600-2613. https://doi.org/10.1021/nn506161j
    Brancolini G, Corazza A, Vuano M, Fogolari F, Mimmi MC, Bellotti V et al. Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein. ACS Nano. 2015 Jan 1;9(3):2600-2613. https://doi.org/10.1021/nn506161j
    Brancolini, Giorgia ; Corazza, Alessandra ; Vuano, Marco ; Fogolari, Federico ; Mimmi, Maria Chiara ; Bellotti, Vittorio ; Stoppini, Monica ; Corni, Stefano ; Esposito, Gennaro. / Probing the influence of citrate-capped gold nanoparticles on an amyloidogenic protein. In: ACS Nano. 2015 ; Vol. 9, No. 3. pp. 2600-2613.
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