Fabio Librizzi

Instituto Biofisika

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Co-Authors

Rita Carrotta

Instituto Biofisika

Silvia Vilasi

Instituto Biofisika

Maria Rosalia Mangione

National Research Council

Maurizio Leone

Mario Negri Institute for Pharmacological Research

Valeria Vetri

University of Palermo

Pier Luigi San Biagio

National Research Council

Vincenzo Martorana

National Research Council

María Grazia Ortore

Marche Polytechnic University

Donatella Bulone

Instituto Biofisika

Caterina Ricci

University of Milan

Cooperative Institutions

University of Palermo

National Research Council

Instituto Biofisika

University of Palermo

National Academies of Sciences, Engineering, and Medicine

National Interuniversity Consortium for the Physical Sciences of Matter

University of Copenhagen

Institute for Biomedical Research and Innovation

Istituto di Biomedicina e di Immunologia Molecolare Alberto Monroy

Czech Academy of Sciences, Institute of Biophysics

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pH effect on thermal aggregation of concanavalin A

Valeria Militello Fabio Librizzi Giovanna Navarra Valeria Vetri Vetri

Source

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Amyloid beta-peptides interaction with a model membrane: can chaperones change the fate?

Marco Maccarini Rita Carrotta Péter Falus Fabio Librizzi Maria Rosalia Mangione

Amyloid (mycology)

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Amyloid β-peptide interaction with GM1 containing model membrane

Advances in biomembranes and lipid self-assembly (2020)

Rita Carrotta Fabio Librizzi Maria Rosalia Mangione Silvia Vilasi Óscar Morán

10.1016/bs.abl.2020.04.001

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α_S1-Casein-Loaded Proteo-liposomes as Potential Inhibitors in Amyloid Fibrillogenesis: In Vivo Effects on a C. elegans Model of Alzheimer’s Disease

ACS Chemical Neuroscience (2023)

Angela Paterna Pamela Santonicola Giulia Di Prima Estella Rao Samuele Raccosta

According to the amyloid hypothesis, in the early phases of Alzheimer's disease (AD), small soluble prefibrillar aggregates of the amyloid β-peptide (Aβ) interact with neuronal membranes, causing neural impairment. Such highly reactive and toxic species form spontaneously and transiently in the amyloid building pathway. A therapeutic strategy consists of the recruitment of these intermediates, thus preventing aberrant interaction with membrane components (lipids and receptors), which in turn may trigger a cascade of cellular disequilibria. Milk αs1-Casein is an intrinsically disordered protein that is able to inhibit Aβ amyloid aggregation in vitro, by sequestering transient species. In order to test αs1-Casein as an inhibitor for the treatment of AD, it needs to be delivered in the place of action. Here, we demonstrate the use of large unilamellar vesicles (LUVs) as suitable nanocarriers for αs1-Casein. Proteo-LUVs were prepared and characterized by different biophysical techniques, such as multiangle light scattering, atomic force imaging, and small-angle X-ray scattering; αs1-Casein loading was quantified by a fluorescence assay. We demonstrated on a C. elegans AD model the effectiveness of the proposed delivery strategy in vivo. Proteo-LUVs allow efficient administration of the protein, exerting a positive functional readout at very low doses while avoiding the intrinsic toxicity of αs1-Casein. Proteo-LUVs of αs1-Casein represent an effective proof of concept for the exploitation of partially disordered proteins as a therapeutic strategy in mild AD conditions.

Nanocarriers

Fibrillogenesis

Amyloid (mycology)

10.1021/acschemneuro.3c00239

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Citations (1)

Light Scattering as an Easy Tool to Measure Vesicles Weight Concentration

Membranes (2020)

Giulia Di Prima Fabio Librizzi Rita Carrotta

Over the last few decades, liposomes have emerged as promising drug delivery systems and effective membrane models for studying biophysical and biological processes. For all applications, knowing their concentration after preparation is crucial. Thus, the development of methods for easily controlling vesicles concentration would be of great utility. A new assay is presented here, based on a suitable analysis of light scattering intensity from liposome dispersions. The method, tested for extrusion preparations, is precise, easy, fast, non-destructive and uses a tiny amount of sample. Furthermore, the scattering intensity can be measured indifferently at different angles, or even by using the elastic band obtained from a standard spectrofluorimeter. To validate the method, the measured concentrations of vesicles of different matrix compositions and sizes, measured by light scattering with different angles and instruments, were compared to the data obtained by the standard Stewart assay. Consistent results were obtained. The light scattering assay is based on the assessment of the mass fraction lost in the preparation, and can be applied for methods such as extrusion, homogenization, French press and other microfluidic procedures.

Homogenization

Matrix (chemical analysis)

10.3390/membranes10090222

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Citations (8)

Optical properties of biocompatible polyaniline nano-composites

Journal of Non-Crystalline Solids (2006)

Clelia Dispenza Maurizio Leone Caterina Lo Presti Fabio Librizzi G. Spadaro

Biocompatibility

Bioelectronics

Biocompatible material

10.1016/j.jnoncrysol.2006.06.017

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Citations (31)

Isolation of extracellular vesicles from microalgae: towards the production of sustainable and natural nanocarriers of bioactive compounds

Biomaterials Science (2021)

Sabrina Picciotto Maria Elena Barone David Fierli Anita Aranyos Giorgia Adamo

Biophysical and biochemical characterisation of microalgae-derived extracellular vesicles.

Nanocarriers

Extracellular Vesicles

Isolation

Sustainable Production

Extracellular vesicles

10.1039/d0bm01696a

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Citations (58)

Effects of confinement on insulin amyloid fibrils formation

European Biophysics Journal (2007)

Fabio Librizzi Vito Foderà Valeria Vetri Caterina Lo Presti Maurizio Leone

Fibrillation

Amyloid (mycology)

10.1007/s00249-007-0137-3

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Citations (23)

Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein

Molecules (2021)

Valeria Guarrasi Giacoma Cinzia Rappa Maria Assunta Costa Fabio Librizzi Marco Raimondo

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology.

Thioflavin

Congo red

Amyloid (mycology)

10.3390/molecules26082371

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Citations (4)

Investigation on Structural Features and Antiaggregation Properties of Chaperonins and Chaperon Like Molecules

Biophysical Journal (2016)

Maria Rosalia Mangione Dario Dpigolon Rosa Passantino Rita Carrotta Fabio Librizzi

Fibrillogenesis

Chaperonin

Co-chaperone

Chaperone (clinical)

Amyloid (mycology)

10.1016/j.bpj.2015.11.1186

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