Review
Biochemistry & Molecular Biology
Laura Acquasaliente, Vincenzo De Filippis
Summary: Amyloidoses are diseases caused by the accumulation of misfolded proteins known as amyloid fibrils in various organs. There are currently 36 different types of amyloidosis, each associated with the misfolding of a specific protein. The aggregation of amyloid-forming proteins can be caused by genetic mutations, environmental factors, excessive concentration, or post-translational modifications. This review focuses on the proteolytic susceptibility of three main amyloidogenic proteins and their connection to intestinal inflammation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Review
Cell Biology
Alessandra Bigi, Roberta Cascella, Cristina Cecchi
Summary: The misfolding and aggregation of a-synuclein is the key feature of synucleinopathies, such as Parkinson's disease and dementia with Lewy bodies. Soluble oligomeric assemblies formed during the early stages of aggregation are toxic to neurons, while fibrillar conformers contribute to the spreading of the pathology. Recent studies have also shown that a-synuclein fibrils release soluble and highly toxic oligomeric species, leading to immediate dysfunction in recipient neurons. This review discusses the mechanisms of cellular dysfunction caused by a-synuclein oligomers and fibrils in synucleinopathies.
NEURAL REGENERATION RESEARCH
(2023)
Review
Biochemistry & Molecular Biology
Liisa Lutter, Liam D. Aubrey, Wei-Feng Xue
Summary: Predicting the highly ordered three-dimensional structures of amyloid protein fibrils from their monomeric self-assembly precursors remains a challenging aspect of the classical protein folding problem, due to the polymorphic nature of amyloid assembly. Understanding the diversity and individuality of amyloid structures, as well as the link to biology and disease phenotypes, is essential. Current research focuses on resolving the structural basis and biological consequences of polymorphic amyloid assemblies using various techniques such as cryo-EM, ssNMR, and AFM.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Article
Biophysics
Victoria T. Reichelderfer, Andres F. Chaparro Sosa, Joel L. Kaar, Daniel K. Schwartz
Summary: The interactions between lipid bilayers and insulin can either stabilize or destabilize the protein, preventing or exacerbating the formation of amyloid fibrils.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2022)
Review
Medicine, General & Internal
Agnieszka Stelmach-Goldys, Monika Zaborek-Lyczba, Jakub Lyczba, Bartosz Garus, Marcin Pasiarski, Paulina Mertowska, Paulina Malkowska, Rafal Hrynkiewicz, Paulina Niedzwiedzka-Rystwej, Ewelina Grywalska
Summary: AL amyloidosis is a systemic disease characterized by the deposition of protein fibers formed from light chains produced by neoplastic clone of plasmocytes. Late diagnosis leads to high mortality rate, and the complex clinical picture and slow progression of the disease contribute to the delayed diagnosis. Early diagnosis and correct identification of the type of amyloidosis are crucial for treatment planning and effectiveness.
JOURNAL OF CLINICAL MEDICINE
(2022)
Article
Biochemical Research Methods
Takahiro Watanabe-Nakayama, Kenjiro Ono
Summary: The structural dynamics of amyloid protein aggregation process play a role in neurodegenerative diseases. High-speed atomic force microscopy (HS-AFM) is a useful tool to visualize individual aggregate species. Correction of stage drift in HS-AFM images can be done using free software like ImageJ, allowing for easier analysis of structural dynamics.
Review
Pharmacology & Pharmacy
Michele Vendruscolo
Summary: Protein misfolding diseases, such as Alzheimer's and Parkinson's diseases, have a major impact on our healthcare systems and societies. This paper discusses drug discovery strategies to target protein misfolding and aggregation, including thermodynamic and kinetic approaches. There is a need for disease-modifying treatments to address the over 50 human disorders associated with protein misfolding and aggregation.
EXPERT OPINION ON DRUG DISCOVERY
(2023)
Review
Biochemistry & Molecular Biology
Jin-Beom Si, Bokyung Kim, Jin Hae Kim
Summary: TTR is a crucial transporter of thyroid hormone and retinol binding protein in human plasma and cerebrospinal fluid, yet it is also known for its amyloidogenic nature leading to various amyloidoses. Research has shown that decreased stability of TTR's native tetrameric conformation is the main cause of these diseases, and recent multidisciplinary investigations have shed light on the mechanistic details of TTR amyloidogenic transformation. Special emphasis has been placed on identifying novel structural features in amyloidogenic species of TTR and discussing the proteolysis-induced fragmentation mechanism that promotes TTR amyloidosis.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Engineering, Chemical
Yanxian Zhang, Yijing Tang, Dong Zhang, Yonglan Liu, Jian He, Yung Chang, Jie Zheng
Summary: The research focuses on the mechanism of amyloid cross-seeding between Aβ and hIAPP and its connection between AD and T2D, explores the role of structural compatibility and sequence similarity of amyloid proteins in cross-seeding, and proposes current challenges and future research directions in this less-studied field.
CHINESE JOURNAL OF CHEMICAL ENGINEERING
(2021)
Review
Biochemistry & Molecular Biology
Hailey B. Penticoff, Hannah K. Hipkiss, Ashley A. Hetak, Dalen W. Agnew, Jessica S. Fortin
Summary: Amyloidosis is a group of protein-folding disorders characterized by amyloid deposits in one or multiple organs. Comparing amyloidosis cases in free-living wild and zoo animals can help determine species susceptible to amyloid formation and commonly involved prone-to-aggregate proteins. Understanding the diversity, transmission, and pathogenesis of amyloidogenic proteins and affected species may aid in preventive interventions and development of new diagnostic and therapeutic strategies.
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
(2021)
Article
Geriatrics & Gerontology
Ines Moreno-Gonzalez, George Edwards, Rodrigo Morales, Claudia Duran-Aniotz, Gabriel Escobedo Jr, Mercedes Marquez, Marti Pumarola, Claudio Soto
Summary: Alzheimer's disease (AD) is one of the leading causes of dementia in late life, and the misfolding and aggregation of amyloid beta (A β) and tau proteins are thought to be hallmark events. Recent studies have shown that small quantities of preformed aggregates can induce protein misfolding and aggregation, similar to the transmission of prion diseases. This study investigated the presence of A β aggregates in the brains of aged cattle and their ability to promote AD pathological features. The findings demonstrate that cows can develop seeding-competent A β aggregates, similar to what is observed in AD patients.
FRONTIERS IN AGING NEUROSCIENCE
(2022)
Article
Spectroscopy
Govindarajan Prasanna, Pu Jing
Summary: This study investigated the remodeling of mature AGEs modified amyloid fibrils by polyphenols through various spectroscopy and microscopy techniques, as well as molecular docking studies. The results showed that polyphenols could transform the secondary structure of amyloid fibrils and remodel them into different aggregate structures through non-covalent interactions. The findings suggest that polyphenols have the potential to alleviate AGEs-mediated amyloidosis.
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
(2021)
Review
Biochemistry & Molecular Biology
Yijing Tang, Dong Zhang, Xiong Gong, Jie Zheng
Summary: This article primarily discusses and summarizes the mechanistic causes of Alzheimer's disease (AD). Different mechanisms of AD could potentially work together to initiate, trigger, and promote the onset and development of the disease. Some of these mechanisms are also applicable to other amyloid diseases, explaining the pathogenesis and pathology spreading among these diseases.
BIOPHYSICAL CHEMISTRY
(2022)
Article
Biotechnology & Applied Microbiology
Xin Chen, Xiaowei Li, Boyang Ji, Yanyan Wang, Olena P. Ishchuk, Egor Vorontsov, Dina Petranovic, Verena Siewers, Martin K. M. Engqvist
Summary: This article investigates the limiting factors in the production of recombinant proteins in industrial microorganisms and identifies genes that can alleviate these factors, leading to a significant increase in recombinant protein production in yeast.
METABOLIC ENGINEERING
(2022)
Article
Biochemistry & Molecular Biology
Meghna Dabur, Joana A. Loureiro, Maria Carmo Pereira
Summary: Amyloidosis is a disease caused by improperly folded proteins accumulating in tissues and damaging organs. It has a significant impact on global health, but there are currently no effective treatments available. However, recent research has shown the potential of fluorine-modified therapeutic molecules and nanoparticles in regulating amyloidogenic proteins.
Article
Nutrition & Dietetics
Timm Intemann, Iris Pigeot, Stefaan De Henauw, Gabriele Eiben, Lauren Lissner, Vittorio Krogh, Katarzyna Deren, Denes Molnar, Luis A. Moreno, Paola Russo, Alfonso Siani, Ivana Sirangelo, Michael Tornaritis, Toomas Veidebaum, Valeria Pala
EUROPEAN JOURNAL OF NUTRITION
(2019)
Article
Cell Biology
Clara Iannuzzi, Margherita Borriello, Antonella D'Agostino, Donatella Cimini, Chiara Schiraldi, Ivana Sirangelo
JOURNAL OF CELLULAR PHYSIOLOGY
(2019)
Article
Cell Biology
Alessia Varone, Stefania Mariggio, Manpreet Patheja, Vincenzo Maione, Antonio Varriale, Mariangela Vessichelli, Daniela Spano, Fabio Formiggini, Matteo Lo Monte, Nadia Brancati, Maria Frucci, Pompea Del Vecchio, Sabato D'Auria, Angela Flagiello, Clara Iannuzzi, Alberto Luini, Piero Pucci, Lucia Banci, Carmen Valente, Daniela Corda
CELL COMMUNICATION AND SIGNALING
(2019)
Article
Nutrition & Dietetics
Ivana Sirangelo, Luigi Sapio, Angela Ragone, Silvio Naviglio, Clara Iannuzzi, Daniela Barone, Antonio Giordano, Margherita Borriello
Article
Biochemistry & Molecular Biology
Ivana Sirangelo, Margherita Borriello, Maria Liccardo, Marika Scafuro, Paola Russo, Clara Iannuzzi
Summary: This study demonstrates that Hydroxytyrosol (HT) selectively inhibits protein glycation reaction and counteracts the cytotoxicity induced by advanced glycation end-products (AGEs) in human neurotypical cells, suggesting its potential as a promising molecule in protecting against neurodegenerative disorders.
Article
Biochemistry & Molecular Biology
Ivana Sirangelo, Maria Liccardo, Clara Iannuzzi
Summary: The major phenolic compound HT in olive oil shows potential in counteracting cardiotoxicity induced by Dox while not interfering with its anti-tumor properties. This study identifies HT as a promising molecule for the development of additional therapeutic approaches to prevent anthracycline-related cardiotoxicity and improve antineoplastic treatments.
Article
Nutrition & Dietetics
Margherita Borriello, Fabio Lauria, Ivana Sirangelo, Krasimira Aleksandrova, Antje Hebestreit, Alfonso Siani, Paola Russo
Summary: This study evaluated the association between urinary fluorescent AGEs and biomarkers of subclinical inflammation in children and adolescents. The results showed a significant positive correlation between urinary AGEs and high-sensitivity C-reactive protein, IL-15, IP-10, and IL-1Ra. Multiple regression analysis demonstrated that urinary AGEs, age, and BMI Z-score were independent variables predicting high-sensitivity C-reactive protein levels. These findings suggest that fluorescent urinary AGEs measurement may serve as a simple, noninvasive, and rapid technique to assess the association between AGEs and biomarkers of inflammation.
Review
Biochemistry & Molecular Biology
Clara Iannuzzi, Maria Liccardo, Ivana Sirangelo
Summary: Nowadays, bioactive natural products are vital for drug development due to their safety and strong antioxidant power. Vanillin, a natural phenolic compound found in vanilla beans, is widely used in various industries. In addition to its industrial applications, vanillin has numerous beneficial effects on human health, such as being an antioxidant and possessing anti-inflammatory, anti-mutagenic, anti-metastatic, and anti-depressant properties. Furthermore, vanillin exhibits neuroprotective effects on neurological disorders and neuropathophysiological conditions. This study reviews the mechanisms by which vanillin prevents neuroinflammation and neurodegeneration, providing the latest insights into its beneficial properties for chronic neurodegenerative diseases.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Salvatore Adinolfi, Rita Puglisi, Jason C. Crack, Clara Iannuzzi, Fabrizio Dal Piaz, Petr V. Konarev, Dmitri I. Svergun, Stephen Martin, Nick E. Le Brun, Annalisa Pastore
FRONTIERS IN MOLECULAR BIOSCIENCES
(2018)
Review
Biophysics
Ivana Sirangelo, Margherita Borriello, Gaetano Irace, Clara Iannuzzi