Oxidative Medicine and Molecular Mechanisms of Thrombosis Laboratory
Research Team’s name: Oxidative Medicine and Molecular Mechanisms of Thrombosis Laboratory
Acronimo e Logo: ThrombOxi Research Lab
Coordinator: Prof. Niccolò Taddei
Brief Biographical sketch of the coordinator
Prof. Niccolò Taddei is Full Professor of Biochemistry (BIOS-07/A) at the University of Florence, where he has developed a distinguished academic career spanning more than three decades. He graduated in Medicine and Surgery with honours in 1987 and obtained his Specialization in Biochemistry and Clinical Chemistry, also with honours, in 1992. His academic progression includes appointments as Researcher (1992), Associate Professor (2000), and Full Professor (2005).
Prof. Taddei has gained significant international research experience through appointments at the University of Oxford and Stockholm University, collaborating with internationally renowned scientists in the fields of protein chemistry and molecular biology.
He is co-author of more than 130 peer-reviewed scientific publications in international journals and has an H-index of 51 (Scopus, 2026). His scientific activity initially focused on protein folding, misfolding, and aggregation mechanisms, generating findings of broad relevance to human disease. More recently, his research has primarily focused on oxidative stress and redox biology in relation to the molecular mechanisms of thrombosis. In particular, his work has investigated oxidative structural and functional modifications of fibrinogen, with the aim of clarifying how redox-dependent changes in this key coagulation protein may alter fibrin formation, clot architecture, and thrombotic tendency. His studies have contributed to defining the impact of fibrinogen oxidation in cardiovascular disorders, highlighting how oxidative damage may influence the prothrombotic state and represent a mechanistic link between redox imbalance and vascular disease. Within this framework, his research has also addressed redox-mediated pathways involved in cardiovascular pathology and their possible diagnostic and therapeutic implications. Overall, these studies have advanced the understanding of how oxidative modifications of fibrinogen and related redox mechanisms contribute to thrombosis and thrombotic disease.
Prof. Taddei has extensive experience in academic leadership and higher education management. He has served as President of the Degree Programme in Nursing, Director of the Specialization School in Clinical Biochemistry, Deputy Director of the Department of Experimental and Clinical Biomedical Sciences “Mario Serio”, and member of several institutional committees. He is currently a Coordinator of the Scientific Board of the PhD Program in Biochemistry and Applied Biology at the University of Florence and teaches Biochemistry in the Medical Degree Programme and postgraduate specialization schools.
Coordinator of the Scientific Board of the PhD Program in Biochemistry and Applied Biology at the University of Florence
Member of the following Scientific Societies
Prof. Taddei is a member of the Italian Society of Biochemistry and Molecular Biology and the The Protein Society, and has also contributed extensively to the authorship, translation, and revision of university and secondary-school textbooks in biochemistry, biology, and chemistry.
Member of editorial board of the following Journals
Research Team
Claudia Fiorillo, PhD, Associate Professor of Clinical Pathology and Clinical Biochemistry
Matteo Becatti, PhD, Associate Professor of Biochemistry
Elvira Giurranna, PhD Student
Alice Nerini, PhD Student
Serena Borghi, Postdoctoral Fellow
Current research interest
Current research interests focus on the molecular mechanisms linking oxidative stress, fibrinogen structural alterations, and thrombosis. A major line of investigation of our group is the study of fibrinogen as a dynamic and highly modifiable coagulation protein whose structural and functional properties can be profoundly altered by oxidative damage and other post-translational modifications (PTMs). We aim to define how these modifications affect fibrinogen conformation, fibrin polymerization, clot architecture, mechanical properties, and susceptibility to fibrinolysis, ultimately promoting the formation of denser, less permeable, and more lysis-resistant thrombi.
Particular attention is devoted to the role of oxidative modifications of fibrinogen in thrombotic disease. Our studies investigate how redox imbalance, driven by inflammatory and cellular sources of reactive oxygen species, induces structural rearrangements in fibrinogen and alters its biological behavior, thereby providing a mechanistic link between oxidative stress and thrombosis. Within this framework, we also examine the contribution of specific PTMs to fibrin clot formation and degradation, with the goal of understanding how fibrinogen heterogeneity influences thrombus stability and persistence in different pathological settings.
Our research is applied to cardiovascular, inflammatory, autoimmune, and metabolic diseases in which thrombosis represents a major clinical complication. These include conditions characterized by systemic inflammation and altered redox homeostasis, where fibrinogen oxidation and abnormal clot properties may contribute to the development of a prothrombotic phenotype. In this context, we investigate fibrinogen-derived structural and functional abnormalities as potential biomarkers of thrombotic risk and disease activity.
A further research objective is the identification of innovative strategies capable of modulating these pathogenic mechanisms. In particular, we explore whether nutritional interventions, anti-inflammatory treatments, and redox-targeted therapeutic approaches can reverse oxidative fibrinogen modifications, restore more physiological clot characteristics, and reduce thrombotic risk. Overall, our work aims to advance the understanding of fibrinogen-centered mechanisms of thrombosis and to translate these findings into clinically relevant diagnostic and therapeutic perspectives.
Key words
Fibrinogen, Thrombosis, Oxidative Stress, Redox Biology, Post-Translational Modifications, Fibrin Clot Structure, Fibrinolysis, Cardiovascular Disease, Biomarkers, Translational Medicine
Current/recent sources of funding
PNRR Tuscan Health Ecosystem – Research Unit Leader (Matteo Becatti)
Organizzazione Toscana Trapianti (PI: Claudia Fiorillo)
10 best pubblications of the last 5 years
1. Prothrombotic profiles in myelofibrosis: Fibrinogen oxidation and the beneficial effects of ruxolitinib. Nencini F, La Spina E, Borghi S, Giurranna E, Argento FR, Fini E, Giallongo C, Duminuco A, Volti GL, Palumbo GA, Taddei N, Fiorillo C, Tibullo D, Becatti M. Thromb Res. 2025 Dec;256:109517. doi: 10.1016/j.thromres.2025.109517.
2. Fibrinogen glycosylation and glycation: molecular insights into thrombosis and vascular disease. Borghi S, Nencini F, Giurranna E, Barbaro I, Taddei N, Fiorillo C, Becatti M. Front Mol Biosci. 2025 Sep 24;12:1680332. doi: 10.3389/fmolb.2025.1680332.
3. Reactive Oxygen Species-Induced Modifications of Fibrin Clots as a Link Between Immune Responses and Atherothrombosis in Systemic Lupus Erythematosus. Becatti M, Emmi G, Bettiol A, Mannucci A, Argento FR, Fini E, Borghi S, Nencini F, Nicastro M, Mattioli I, Silvestri E, Vaglio A, Prisco D, Fiorillo C. Arthritis Rheumatol. 2026 Feb;78(2):344-356. doi: 10.1002/art.43371.
4. Fibrinogen Structural Changes and Their Potential Role in Endometriosis-Related Thrombosis. Fini E, Argento FR, Borghi S, Giurranna E, Nencini F, Cirillo M, Fatini C, Taddei N, Coccia ME, Fiorillo C, Becatti M. Antioxidants (Basel). 2024 Nov 27;13(12):1456. doi: 10.3390/antiox13121456.
5. Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation. Nencini F, Bettiol A, Argento FR, Borghi S, Giurranna E, Emmi G, Prisco D, Taddei N, Fiorillo C, Becatti M. Mol Biomed. 2024 Oct 31;5(1):45. doi: 10.1186/s43556-024-00214-x.
6. Oxidative stress-induced fibrinogen modifications in liver transplant recipients: unraveling a novel potential mechanism for cardiovascular risk. Gitto S, Fiorillo C, Argento FR, Fini E, Borghi S, Falcini M, Roccarina D, La Delfa R, Lillo L, Zurli T, Forte P, Ghinolfi D, De Simone P, Chiesi F, Ingravallo A, Vizzutti F, Aspite S, Laffi G, Lynch E, Petruccelli S, Carrai P, Palladino S, Sofi F, Stefani L, Amedei A, Baldi S, Toscano A, Lau C, Marra F, Becatti M. Res Pract Thromb Haemost. 2024 Aug 23;8(6):102555. doi: 10.1016/j.rpth.2024.102555.
7. Advancing Thrombosis Research: A Novel Device for Measuring Clot Permeability. Landi E, Mugnaini M, Vatansever T, Fort A, Vignoli V, Giurranna E, Argento FR, Fini E, Emmi G, Fiorillo C, Becatti M. Sensors (Basel). 2024 Jun 9;24(12):3764. doi: 10.3390/s24123764.
8. ROS-driven structural and functional fibrinogen modifications are reverted by interleukin-6 inhibition in Giant Cell Arteritis. Bettiol A, Argento FR, Fini E, Bello F, Di Scala G, Taddei N, Emmi G, Prisco D, Becatti M, Fiorillo C. Thromb Res. 2023 Oct;230:1-10. doi: 10.1016/j.thromres.2023.08.011.
9. Neutrophil-mediated mechanisms of damage and in-vitro protective effect of colchicine in non-vascular Behçet's syndrome. Bettiol A, Becatti M, Silvestri E, Argento FR, Fini E, Mannucci A, Galora S, Mattioli I, Urban ML, Malandrino D, Palermo A, Taddei N, Emmi G, Prisco D, Fiorillo C.Clin Exp Immunol. 2021 Dec;206(3):410-421. doi: 10.1111/cei.13664.
10. Butyrate-Rich Diets Improve Redox Status and Fibrin Lysis in Behçet's Syndrome. Emmi G, Bettiol A, Niccolai E, Ramazzotti M, Amedei A, Pagliai G, Taddei N, Sofi F, Fiorillo C, Prisco D, Becatti M. Circ Res. 2021 Jan 22;128(2):278-280. doi: 10.1161/CIRCRESAHA.120.317789.
Previous research experiences
Previous research activities of the group were mainly focused on protein chemistry, structural biochemistry, and the molecular mechanisms regulating protein folding, misfolding, and aggregation. In particular, early studies investigated proteins of the acylphosphatase family and structurally related models, contributing to the identification of key physicochemical determinants (such as hydrophobicity, net charge, and β-sheet propensity) that govern protein aggregation processes. These findings provided relevant insights into general mechanisms of amyloid formation and protein misfolding disorders. The group also explored, through biophysical approaches, the influence of specific amino acid residues on protein stability, folding pathways, and aggregation tendency. Additional studies examined the effects of non-protein molecules, including lipids and glycosaminoglycans, on protein aggregation, helping to clarify how the tissue microenvironment modulates pathological protein deposition. These earlier experiences generated strong expertise in protein purification, conformational analysis, spectroscopy, enzymology, and structure-function relationships, which later became the methodological foundation for subsequent translational studies on oxidative stress, fibrinogen structure, and thrombosis.
Main scientific contributions
The research activity of the group has significantly contributed to the understanding of the molecular links between oxidative stress, inflammation, fibrinogen structure, and thrombosis. A major achievement has been the demonstration that reactive oxygen species induce structural and functional alterations of fibrinogen, leading to abnormal fibrin polymerization, denser clot architecture, reduced clot permeability, and impaired susceptibility to fibrinolysis. These findings identified fibrinogen oxidation as a novel mechanism promoting thrombus formation and persistence. The group has further clarified the role of inflammatory leukocytes, particularly neutrophils, as major cellular sources of oxidative stress capable of driving fibrinogen damage and thrombosis. In Behçet’s syndrome, it demonstrated that neutrophil NADPH oxidase activation promotes fibrinogen oxidation and contributes to inflammation-induced thrombosis, providing mechanistic support for immunomodulatory approaches in thrombotic vasculitis. Another important contribution has been the extension of these mechanisms to different clinical settings characterized by increased cardiovascular risk. The group showed that oxidative fibrinogen structure is associated with prothrombotic clot abnormalities in myocardial infarction, cirrhosis, giant cell arteritis, and systemic lupus erythematosus, thereby establishing fibrinogen as a common molecular target linking redox imbalance to thrombosis across inflammatory and non-inflammatory diseases. The team has also provided relevant methodological advances through the application of circular dichroism spectroscopy, intrinsic fluorescence analysis, confocal and STED super-resolution microscopy to characterize fibrinogen conformational changes and fibrin network ultrastructure in human disease. These approaches enabled direct visualization of pathogenic clot remodeling at the molecular and structural level. Finally, the group has translated mechanistic findings into preventive strategies, demonstrating that nutritional interventions such as Mediterranean, vegetarian, and butyrate-enriched diets can improve redox balance and modulate thrombosis-related pathways, supporting lifestyle-based approaches for cardiovascular prevention.
Collaborations
Prof. Domenico Prisco, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Giacomo Emmi, Department of Medical, Surgery and Health Sciences, University of Trieste, Trieste, Italy.
Prof. Elena Silvestri, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Francesco Sofi, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Amedeo Amedei, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Stefano Gitto, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Gabriella Tedeschi, Department of Veterinary Medicine and Animal Sciences (DIVAS), University of Milan, Lodi, Italy.
Prof. Francesco Piazza, Department of Physics and Astronomy, University of Florence, Italy
Prof. Daniela Braconi, Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Italy.
Prof. Laura Stefani, Sports Medicine Center, University of Florence, Italy.
Prof. Ada Fort, Department of Information Engineering and Mathematics, University of Siena, Italy.
Prof. Marco Mugnaini, Department of Information Engineering and Mathematics, University of Siena, Italy.
Prof. Luisella Cianferotti, Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Italy.
Prof. Maria Elisabetta Coccia, Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Italy.
Prof. Annamaria Morelli, Department of Experimental and Clinical Medicine, University of Florence, Italy.
Prof. Tania Gamberi, Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Italy.
Prof. Francesca Magherini, Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Italy.
Ultimo aggiornamento
29.04.2026