Article
Multidisciplinary Sciences
Mantas Ziaunys, Andrius Sakalauskas, Kamile Mikalauskaite, Vytautas Smirnovas
Summary: Protein aggregation is considered a major cause of several neurodegenerative diseases. Despite progress in amyloid research, the process of fibrillization remains not fully understood. Tracking insulin aggregation using ThT reveals anomalous double-sigmoidal kinetics, likely related to ThT-positive intermediates, which do not significantly alter the overall aggregation process.
Article
Chemistry, Physical
Akshat M. Desai, Shrishti P. Pandey, Prabhat K. x Singh
Summary: This study investigated the influence of different counter-anions on the aggregation of the cationic amyloid sensing probe Thioflavin-T (ThT), revealing distinct ion behaviors in the organization process. Optical properties of the salt-induced aggregates were characterized using detailed emission and absorption measurements, and the formation of contact ion pairs was explained through the theory of matching water affinity. These findings suggest that the selection of counterions with appropriate sizes can induce aggregation of ThT and potentially help in detecting false positive signals in high ionic strength environments.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2021)
Article
Chemistry, Physical
Debanjan Bagchi, Avijit Maity, Soumya Kanti De, Anjan Chakraborty
Summary: For the first time, this study reports the existence of different metastable intermediate states during the self-assembly process of phenylalanine in the presence of various metal ions. The metal ion-amino acid interactions lead to the initial formation of spherical aggregates, which then transform into other structures. These findings contribute to a better understanding of the role of metal ions in amino acid self-assembly.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2022)
Article
Biotechnology & Applied Microbiology
Wenjia Lou, Samuel D. Stimple, Alec A. Desai, Emily K. Makowski, Sibel Kalyoncu, Jesper E. Mogensen, Lotte T. Spang, Desiree J. Asgreen, Arne Staby, Karen Duus, Jan Amstrup, Yulei Zhang, Peter M. Tessier
Summary: Biologics such as peptides and proteins have attractive attributes, but are prone to aggregation. By developing conformation-specific antibodies, a sensitive immunoassay for detecting aggregates has been successfully created. These antibodies not only exhibit high conformational specificity, but also cross-react with amyloid fibrils formed by various polypeptides.
BIOTECHNOLOGY AND BIOENGINEERING
(2021)
Article
Chemistry, Analytical
Kentaro Noi, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto, Hirotsugu Ogi
Summary: The disassembly activity of anthocyanins on Aβ fibrils depends on the number of hydroxyl groups in the six-membered ring B of anthocyanin, with only delphinidin-3-galactoside showing high disassembly activity due to possessing three hydroxyl groups there. Results demonstrate the importance of the number of hydroxyl groups and highlight the usefulness of TIRFM-QCM as a powerful tool in studying interactions between amyloid fibrils and compounds.
ANALYTICAL CHEMISTRY
(2021)
Article
Biotechnology & Applied Microbiology
Jesus Camara-Almiron, Laura Dominguez-Garcia, Nadia El Mammeri, Alons Lends, Birgit Habenstein, Antonio de Vicente, Antoine Loquet, Diego Romero
Summary: This study demonstrates that recombinantly purified RcTasA retains the biochemical properties of the entire protein and shows that two aggregation-prone stretches and imperfect amino acid repeats in RcTasA contribute to its amyloid-like capacity. The study also identifies the critical role of residues D64, K68, and D69 in the structural function of TasA. Experiments with mutant versions of TasA reveal a partial loss of function in the assembly of the extracellular matrix or the stability of the core and amyloid-like properties. Overall, these findings provide insights into the polymerization process of TasA and the sequence determinants that govern the behavior of protein filaments in bacteria.
NPJ BIOFILMS AND MICROBIOMES
(2023)
Article
Chemistry, Multidisciplinary
M. Rodrigues, P. Bhattacharjee, A. Brinkmalm, D. T. Do, C. M. Pearson, S. De, A. Ponjavic, J. A. Varela, K. Kulenkampff, I Baudrexel, D. Emin, F. S. Ruggeri, J. E. Lee, A. R. Carr, T. P. J. Knowles, H. Zetterberg, T. N. Snaddon, S. Gandhi, S. F. Lee, D. Klenerman
Summary: This study presents a method called "amyloid precipitation" to capture amyloid-containing aggregates in human biofluids in an unbiased way. By using a specific structure-specific chemical dimer, the researchers were able to target the amyloid structure of all protein aggregates present in human cerebrospinal fluid, isolate them for analysis, and characterize them using single-molecule fluorescence imaging and mass spectrometry.
Article
Chemistry, Physical
Beeta Kumari, Manisha Yadav, Manoj Kumar, Pratibha Kushwaha, Rajesh Kumar
Summary: The macromolecular crowding effect transforms acid-denatured ferricytochrome c (cyt cIII) (UA-state) to molten-globule (MGMC-state) at pH 1.85. The magnitudes of crowding-induced stabilization free energy (∆G) and preferential hydration (∆ΓW) were found to be decreased as the size and shape of the crowder towards refolding and stabilization of UA-state to MGMC-state. Macromolecular crowding increased the thermodynamic stability of acid-denatured cyt cIII and the size and shape of crowder control the crowding-induced thermodynamic stabilization of MGMC-state.
JOURNAL OF MOLECULAR LIQUIDS
(2023)
Article
Polymer Science
Malgorzata Milewska, Andrzej Milewski, Ilona Wandzik, Martina H. Stenzel
Summary: Trehalose glycopolymers have been extensively studied recently and have shown some unique properties. In order to compare their properties, researchers synthesized structurally similar glycopolymers composed of trehalose and sucrose. These glycopolymers have very low content of non-saccharide structural fragments, making their properties strongly influenced by the saccharide moieties. The study comprehensively characterized the glycopolymers, including their tendency to self-assemble, hydrolytic stabilities at different pH, and susceptibility to enzymatic hydrolysis.
Article
Multidisciplinary Sciences
Kritika Kumari, Gurumayum Suraj Sharma, Akshita Gupta, Khuraijam Surjalal Singh, Laishram Rajendrakumar Singh
Summary: Deposition of high-order protein oligomers is a common hallmark of human diseases. In this study, new protein oligomers of Ribonuclease-A and Lysozyme that contain functionally active fractions were identified. These results suggest the existence of such oligomers as protein sinks that may sequester toxic homocysteines in humans.
SCIENTIFIC REPORTS
(2023)
Article
Chemistry, Analytical
Jasvir Kaur, Prabhat K. Singh
Summary: In this study, a simple, convenient, rapid and selective method using a molecular rotor probe Thioflavin-T (ThT) has been developed to detect sodium hexa-meta-phosphate (HMP) in food. The sensing method is based on the aggregation induced emission of ThT by HMP, resulting in the formation of a fluorescent ThT-HMP aggregate complex. The method showed high selectivity and sensitivity towards HMP, and was successfully applied to detect HMP in real water samples.
MICROCHEMICAL JOURNAL
(2022)
Article
Chemistry, Applied
Mirjana Radomirovic, Simeon Minic, Dragana Stanic-Vucinic, Milan Nikolic, Sam Van Haute, Andreja Rajkovic, Tanja Cirkovic Velickovic
Summary: The covalent modification of beta-lactoglobulin (BLG) with phycocyanobilin (PCB) enhances its antioxidant properties and reduces its susceptibility to aggregation, while also improving its resistance to digestive enzymes.
FOOD HYDROCOLLOIDS
(2022)
Article
Chemistry, Multidisciplinary
Elena Sanna, Margarida Rodrigues, Steven G. Fagan, Timothy S. Chisholm, Klara Kulenkampff, David Klenerman, Maria Grazia Spillantini, Franklin I. Aigbirhio, Christopher A. Hunter
Summary: The development of reagents that can bind protein aggregates related to neurodegenerative diseases such as Alzheimer's and Parkinson's is crucial for early disease diagnosis. By linking two benzothiazole aniline head groups with different length polyethylene glycol spacers, fluorescent probes with high affinity for amyloid fibrils have been obtained. These compounds have shown promise in imaging neurodegenerative disease-related protein aggregates in vitro and in postmortem brain tissue.
Article
Chemistry, Organic
Shantanu Sen, Rafat Ali, Harminder Singh, Akanksha Onkar, Pratibha Bhadauriya, Subramaniam Ganesh, Sandeep Verma
Summary: Insulin can form toxic fibrils during production and transportation, which can cause amyloid deposits at injection sites in diabetic patients. It is challenging to distinguish early fibrils from non-fibrillated insulin. This study introduces a modified insulin derivative with a visible color change upon aggregation, allowing for easy assessment of insulin quality.
ORGANIC & BIOMOLECULAR CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Kazuma Murakami, Shiori Horii, Mizuho Hanaki, Kazuhiro Irie
Summary: The aggregation of Amyloid beta 42 in Alzheimer's disease involves nucleation and elongation phases. An orcein derivative, O4, has been shown to convert toxic oligomers into inert fibrils. Screening natural products for compounds that delay nucleation and promote elongation revealed several candidates that reduce the toxicity of Amyloid beta 42 against neuroblastoma cells. These compounds may interact with Amyloid beta 42 to shift its equilibrium from toxic oligomers to inert fibrils.
ACS CHEMICAL NEUROSCIENCE
(2021)
Article
Biochemistry & Molecular Biology
Caterina Ricci, Maria Grazia Ortore, Silvia Vilasi, Rita Carrotta, Maria Rosalia Mangione, Donatella Bulone, Fabio Librizzi, Francesco Spinozzi, Giosalba Burgio, Heinz Amenitsch, Pier Luigi San Biagio
BIOPHYSICAL CHEMISTRY
(2016)
Article
Biochemistry & Molecular Biology
Maria Carmela Nicastro, Dario Spigolon, Fabio Librizzi, Oscar Moran, Maria Grazia Ortore, Donatella Bulone, Pier Luigi San Biagio, Rita Carrotta
BIOPHYSICAL CHEMISTRY
(2016)
Article
Biophysics
Maria Assunta Costa, Maria Rosalia Mangione, Radha Santonocito, Rosa Passantino, Daniela Giacomazza, Fabio Librizzi, Oscar Moran, Rita Carrotta
COLLOIDS AND SURFACES B-BIOINTERFACES
(2018)
Article
Biochemistry & Molecular Biology
R. Carrotta, C. Canale, A. Diaspro, A. Trapani, P. L. San Biagio, D. Bulone
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
(2012)
Article
Biochemistry & Molecular Biology
Claudio Canale, Silvia Seghezza, Silvia Vilasi, Rita Carrotta, Donatella Bulone, Alberto Diaspro, Pier Luigi San Biagio, Silvia Dante
BIOPHYSICAL CHEMISTRY
(2013)
Article
Chemistry, Physical
Rita Carrotta, Silvia Vilasi, Fabio Librizzi, Vincenzo Martorana, Donatella Bulone, Pier Luigi San Biagio
JOURNAL OF PHYSICAL CHEMISTRY B
(2012)
Article
Chemistry, Physical
Fabio Librizzi, Rita Carrotta, Dario Spigolon, Donatella Bulone, Pier Luigi San Biagio
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2014)
Article
Physics, Condensed Matter
C. Corsale, R. Carrotta, M. R. Mangione, S. Vilasi, A. Provenzano, G. Cavallaro, D. Bulone, P. L. San Biagio
JOURNAL OF PHYSICS-CONDENSED MATTER
(2012)
Article
Multidisciplinary Sciences
Silvia Vilasi, Rita Carrotta, Maria Rosalia Mangione, Claudia Campanella, Fabio Librizzi, Loredana Randazzo, Vincenzo Martorana, Antonella Marino Gammazza, Maria Grazia Ortore, Annalisa Vilasi, Gabriella Pocsfalvi, Giosalba Burgio, Davide Corona, Antonio Palumbo Piccionello, Giovanni Zummo, Donatella Bulone, Everly Conway de Macario, Alberto J. L. Macario, Pier Luigi San Biagio, Francesco Cappello
Article
Multidisciplinary Sciences
Fabio Librizzi, Rita Carrotta, Judith Peters, Antonio Cupane
SCIENTIFIC REPORTS
(2018)
Article
Chemistry, Physical
Caterina Ricci, Marco Maccarini, Peter Falus, Fabio Librizzi, Maria Rosalia Mangione, Oscar Moran, Maria Grazia Ortore, Ralf Schweins, Silvia Vilasi, Rita Carrotta
JOURNAL OF PHYSICAL CHEMISTRY B
(2019)
Article
Biochemistry & Molecular Biology
Silvia Vilasi, Rita Carrotta, Caterina Ricci, Giacoma Cinzia Rappa, Fabio Librizzi, Vincenzo Martorana, Maria Grazia Ortore, Maria Rosalia Mangione
ACS CHEMICAL NEUROSCIENCE
(2019)
Article
Biochemistry & Molecular Biology
Giulia Di Prima, Fabio Librizzi, Rita Carrotta
Article
Biology
Rita Carrotta, Maria Rosalia Mangione, Fabio Librizzi, Oscar Moran
Summary: The early impairments in Alzheimer's disease are related to neuronal membrane damage. Different lipids, such as sphingomyelin, cholesterol, and ganglioside GM1, interact with each other and with the A beta peptide. This study used small angle X-ray scattering to investigate these interactions in model membrane systems, specifically large unilamellar liposomes. The analysis revealed concentration-dependent effects of GM1 on membrane thickness and its interaction with A beta peptide, as well as the inhibiting effect of sphingomyelin on the GM1-A beta interaction.
Article
Biochemistry & Molecular Biology
Caterina Ricci, Rita Carrotta, Giacoma Cinzia Rappa, Maria Rosalia Mangione, Fabio Librizzi, Pier Luigi San Biagio, Heinz Amenitsch, Maria Grazia Ortore, Silvia Vilasi
BIOPHYSICAL CHEMISTRY
(2017)