Article
Biochemistry & Molecular Biology
Zigmantas Toleikis, Mantas Ziaunys, Lina Baranauskiene, Vytautas Petrauskas, Kristaps Jaudzems, Vytautas Smirnovas
Summary: The presence of S100A9 alters the aggregation kinetics of alpha-synuclein and stabilizes a specific amyloid fibril structure. The ionic strength of the solution influences the interaction between S100A9 and alpha-synuclein, stabilizing a different structure of alpha-synuclein fibrils.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Zigmantas Toleikis, Raitis Bobrovs, Agne Janoniene, Alons Lends, Mantas Ziaunys, Ieva Baronaite, Vytautas Petrauskas, Kristine Kitoka, Vytautas Smirnovas, Kristaps Jaudzems
Summary: S100A9 interacts with α-synuclein and influences the aggregation process. This study analyzed the interaction using F-19 and 2D N-15-H-1-HSQC NMR spectroscopy and studied the aggregation properties of these two proteins. The results showed that α-synuclein interacts with S100A9 at specific regions, which are also essential in the first step of aggregation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Chemistry, Applied
Yuying Fu, Yuan Li, Shuni Weng, Wenhui Qi, Huanhuan Su, Teng Li
Summary: Ice recrystallization inhibition (IRI) activity of amyloid protein fibrils (APFs) is greatly enhanced when APFs serve as Pickering emulsion stabilizer. The IRI activity resulted from the adsorbed APFs on the surface of emulsion droplets, which showed larger particle size and a higher number of droplets per unit volume. The enhancement of IRI activity caused by oil-water interface adsorption is reasonably ascribed to enlarged size, crowding of APFs on the surface of emulsion droplets, and enhanced ice adsorption of APFs. These findings shed light on the application of IRI-active materials as emulsifiers to improve the quality of frozen food containing emulsions.
FOOD HYDROCOLLOIDS
(2023)
Article
Chemistry, Physical
Uliana Tarabara, Elena Kirilova, Georgiy Kirilov, Kateryna Vus, Olga Zhytniakivska, Valeriya Trusova, Galyna Gorbenko
Summary: Amyloid fibrils can serve as a molecular framework for multi-step Forster resonance energy transfer (msFRET). Novel benzanthrone dyes are being explored as potential mediators of msFRET in insulin amyloid fibrils. The study aims to evaluate the effectiveness of these dyes in detecting amyloid fibrils.
JOURNAL OF MOLECULAR LIQUIDS
(2021)
Article
Chemistry, Multidisciplinary
Uma Sankar Mondal, Subhankar Paul
Summary: Amyloid fibrillation is a major cause of neurological disorders and despite numerous therapeutic approaches, there is no effective therapy available. This study investigated the effect of self-assembled nanostructured lysozyme (snLYZ) and graphene oxide conjugate (GO-snLYZ) on the fibrillation process of HEWL. It was found that snLYZ and GO-snLYZ successfully inhibited the fibril formation, while another protein nanoparticle, nBSA, had minimal inhibitory effect. The inhibition of lysozyme fibrillation was associated with the formation of thinner and smaller fibril fragments.
NEW JOURNAL OF CHEMISTRY
(2023)
Article
Chemistry, Multidisciplinary
Uma Sankar Mondal, Subhankar Paul
Summary: Recent studies have shown that nanomaterials, such as self-assembled nanostructured lysozyme (snLYZ) and graphene oxide conjugate (GO-snLYZ), can effectively inhibit the amyloid fibrillation process of proteins. Inhibition is achieved through protein binding and the formation of aggregated complexes.
NEW JOURNAL OF CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Yuying Fu, Yuan Li, David W. Everett, Shuni Weng, Yun Zhai, Mengtin Wang, Teng Li
Summary: This study employed octenyl succinic anhydride (OSA) modification to improve the dispersibility and ice recrystallization inhibition activity of amyloid proteins fibrils (APFs). The modification mainly reacted with the amino groups of APFs without significantly changing their morphology. The modified fibrils had lower pI, carried more negative charges, and were more hydrophobic. The OSA modification showed a pH-dependent effect on the dispersibility of the fibrils, with stronger aggregation at acidic pH values.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Chemistry, Multidisciplinary
Lanlan Yu, Ruonan Wang, Shucong Li, Ufuoma I. Kara, Eric C. Boerner, Boyuan Chen, Feiyi Zhang, Zhongyi Jian, Shuyuan Li, Mingwei Liu, Yang Wang, Shuli Liu, Yanlian Yang, Chen Wang, Wenbo Zhang, Yuxing Yao, Xiaoguang Wang, Chenxuan Wang
Summary: Scanning tunneling microscopy (STM) is used to distinguish 18 coexisting conformational substates of the β-strand of hIAPP 8-37 and analyze the peptide-peptide interactions. This method also validates the existence of multiple conformations in other β-sheet peptide assemblies. The results provide insights into the conformational ensemble and interpeptide interactions in β-sheet peptide assembly.
ACS CENTRAL SCIENCE
(2023)
Article
Polymer Science
Carlos Noble Jesus, Rhys Evans, Joe Forth, Carolina Estarellas, Francesco Luigi Gervasio, Giuseppe Battaglia
Summary: The study presents the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. The inclusion of aromatic amino acids in the histidine block leads to the formation of amyloid-like fibrils with distinct antiparallel beta-strands. The structures undergo self-assembly in response to pH changes, offering potential for biotechnological and biomedical applications with pH-responsive fibrils in a physiologically relevant range.
Article
Chemistry, Multidisciplinary
Qiantao Song, Yi Li, Zhicheng Jin, Hai Liu, Matthew N. Creyer, Wonjun Yim, Yanping Huang, Xiaobing Hu, Tengyu He, Yajuan Li, Shana O. Kelley, Lingyan Shi, Jiajing Zhou, Jesse V. Jokerst
Summary: This study reports the mild and unique formation of luminescent spherulites at room temperature using benzene-1,4-dithiol. These spherulites not only exhibit robust structure but also show broad clusterization-triggered emission. They also demonstrate biocompatibility and efficient cellular uptake, making them valuable as traceable drug carriers.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Biochemical Research Methods
Mantas Ziaunys, Kamile Mikalauskaite, Andrius Sakalauskas, Vytautas Smirnovas
Summary: The aggregation of amyloidogenic proteins is related to various diseases, with limited treatment options currently available. The challenge in the discovery of potential anti-amyloid molecules lies in identifying the actual inhibitors from complex mixtures. This study successfully scavenged potential aggregation-inhibiting molecules from different compounds and effectively separated them from the aggregates.
BIOTECHNOLOGY JOURNAL
(2021)
Article
Biochemistry & Molecular Biology
Tongtong Hou, Nan Zhang, Chaoren Yan, Minling Ding, Huizhe Niu, Ping Guan, Xiaoling Hu
Summary: This study developed a curcumin lysozyme-imprinted nanosphere (CUR-MIMS) that effectively inhibited the aggregation of lysozyme and showed good biocompatibility, demonstrating its potential as a therapeutic platform for amyloidosis.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biochemistry & Molecular Biology
Govindarajan Prasanna, Pu Jing
Summary: The peptide sequence of A beta(1-11) modulates amyloid fibril formation and interacts with factor XII in Alzheimer's disease. Self-assembly of N-terminal A beta(1-11) into nanotubes and inhibition of amyloid fibrils by polyphenols were studied using various techniques, highlighting the potential therapeutic role of polyphenols in Alzheimer's disease.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Neurosciences
Yuniesky Andrade-Talavera, Gefei Chen, Jonathan Pansieri, Luis Enrique Arroyo -Garcia, Zigmantas Toleikis, Vytautas Smirnovas, Jan Johansson, Ludmilla Morozova-Roche, Andre Fisahn
Summary: This study demonstrates that recombinant Bri2 BRICHOS effectively inhibits the amyloid growth of S100A9 by capping amyloid fibrils. It also shows that both native S100A9 and amyloids of S100A9 disrupt gamma oscillation power and rhythmicity in the hippocampal area, which is associated with Toll-like receptor 4 (TLR4) activation. The co-aggregation of S100A9 with Bri2 BRICHOS prevents the degradation of gamma oscillations.
PROGRESS IN NEUROBIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Mantas Ziaunys, Andrius Sakalauskas, Tomas Sneideris, Vytautas Smirnovas
Summary: Protein aggregation into amyloid fibrils is associated with various disorders, but the mechanisms behind the conversion of non-harmful proteins into such aggregates are not fully understood. Recent studies suggest that multiple types of protein aggregates may co-exist in tissues of patients with amyloid-related disorders, potentially influencing each other.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Mantas Ziaunys, Kamile Mikalauskaite, Dominykas Veiveris, Andrius Sakalauskas, Vytautas Smirnovas
Summary: The interaction between amyloidogenic proteins plays a crucial role in the onset and progression of amyloidoses, yet the cross-interaction between different proteins remains insufficiently understood.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2022)
Article
Chemistry, Multidisciplinary
Madhu Nagaraj, Zahra Najarzadeh, Jonathan Pansieri, Henrik Biverstal, Greta Musteikyte, Vytautas Smirnovas, Steve Matthews, Cecilia Emanuelsson, Janne Johansson, Joel N. Buxbaum, Ludmilla Morozova-Roche, Daniel E. Otzen
Summary: The study analyzes the impact of four different human chaperones on the aggregation process of functional amyloids in bacterial biofilms, showing that they primarily target primary nucleation during fibrillation rather than elongation or secondary nucleation, and the inhibition efficiency is correlated with their affinity for monomeric CsgA and FapC.
Article
Engineering, Environmental
Mohamed Essalhi, Norafiqah Ismail, Solomon Tesfalidet, Jun Pan, Qian Wang, Zhoaliang Cui, M. C. Garcia-Payo, Mohamed Khayet, Jyri-Pekka Mikkola, Shokat Sarmad, Denis Bouyer, Yun Zhao, Baohua Li, C. Andre Ohlin, Naser Tavajohi
Summary: By using CO2 as a non-solvent additive, PVDF membranes were prepared by phase inversion, which showed high performance in desalination and treatment of simulated nuclear wastewater. This method avoids the harmful impact on the environment and represents a decisive step towards sustainability.
CHEMICAL ENGINEERING JOURNAL
(2022)
Article
Biochemistry & Molecular Biology
Saeid Hadi Ali Janvand, Lucy Kate Ladefoged, Asta Zubriene, Andrius Sakalauskas, Gunna Christiansen, Virginija Dudutiene, Birgit Schiott, Daumantas Matulis, Vytautas Smirnovas, Daniel E. Otzen
Summary: Fluorinated sulfonamide compounds can inhibit the formation of amyloid fibrils, potentially providing therapeutic effects against amyloid-related disorders such as Parkinson's, Alzheimer's, and type 2 diabetes, possibly by maintaining insulin in its native monomeric state.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Zeljko M. Svedruzic, Vesna Sendula Jengic, Lucija Ostojic
Summary: By conducting multiscale molecular dynamics studies, we found that an increase in gamma-secretase saturation with its substrate can lead to parallel binding of different substrate molecules at the docking site and active site, inhibiting catalytic activity and increasing the production of longer, more hydrophobic, and more toxic A beta proteins. Similar disruptions in presenilin structures can be observed with different drugs and disease-causing mutations. The C99-beta CTF-APP substrate and beta-secretase pathway may be more toxic than the C83-alpha CTF-APP substrate and alpha-secretase pathway. Nicastrin can control toxic aggregation in the closed conformation, and binding of the C99-beta CTF-APP substrate to gamma-secretase can be controlled by substrate channeling between nicastrin and beta-secretase.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Review
Biochemistry & Molecular Biology
Tahereh Sohrabi, Behnaz Mirzaei-Behbahani, Ramin Zadali, Mitra Pirhaghi, Ludmilla A. Morozova-Roche, Ali Akbar Meratan
Summary: Parkinson's disease (PD) is a common neurological movement disorder characterized by the loss of dopaminergic neurons in the brain. A misfolded protein called a-synuclein (a-syn) has been identified as a key factor in the development of PD. This review discusses the mechanisms by which a-syn dysfunction leads to mitochondrial dysfunction, and the potential therapeutic approaches, such as antioxidant-based therapy, in PD treatment. The review emphasizes the importance of understanding the role of mitochondrial dysfunction in PD pathogenesis.
JOURNAL OF MOLECULAR BIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Rimgaile Tamulyte, Evelina Jankaityte, Zigmantas Toleikis, Vytautas Smirnovas, Marija Jankunec
Summary: Pro-inflammatory, calcium-binding protein S100A9 is involved in neuroinflammation associated with Alzheimer's disease. The protein accumulates on negatively charged lipid bilayers but does not affect the integrity of the bilayer. Understanding the function and interactions of S100A9 may lead to new diagnostic and therapeutic approaches for AD.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
(2023)
Article
Biochemistry & Molecular Biology
Darius Sulskis, Greta Sneideriene, Mantas Ziaunys, Vytautas Smirnovas
Summary: Transmissive spongiform encephalopathies (TSE) are neurodegenerative diseases caused by infectious prions. The species barrier between human and hamster prion proteins was investigated, and it was found that differences in the amino acid sequence in the 82-alpha 2 loop region contribute to the barrier. The study enhanced our understanding of prion-related disease development.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Mantas Ziaunys, Kamile Mikalauskaite, Lukas Krasauskas, Vytautas Smirnovas
Summary: Protein aggregation into amyloid fibrils plays a role in neurodegenerative diseases such as Alzheimer's and Parkinson's. Despite significant research, the process remains poorly understood, hindering the development of treatments. Recent reports of cross-interactions between amyloidogenic proteins, including Tau and prion, have further complicated the process. This study observed a conformation-specific association between Tau and prion fibrils, increasing their aggregate formation and amyloid binding capacity.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Multidisciplinary Sciences
Elina Berntsson, Faraz Vosough, Teodor Svantesson, Jonathan Pansieri, Igor A. Iashchishyn, Lucija Ostojic, Xiaolin Dong, Suman Paul, Juri Jarvet, Per M. Roos, Andreas Barth, Ludmilla A. Morozova-Roche, Astrid Graslund, Sebastian K. T. S. Warmlander
Summary: Alzheimer's disease is the most common cause of dementia worldwide. It is characterized by the presence of insoluble amyloid plaques in the brain, mainly composed of aggregated amyloid-beta (A beta) peptides. Metal homeostasis is altered in AD, and elevated levels of metals such as Cu, Fe, and Zn have been observed in AD plaques. However, the role of metal ions, such as Ni(II), in AD pathology remains unclear.
SCIENTIFIC REPORTS
(2023)
Article
Biochemistry & Molecular Biology
Ella Sanders, Rebecca Csondor, Darius Sulskis, Ieva Baronaite, Vytautas Smirnovas, Luckshi Maheswaran, Jack Horrocks, Rory Munro, Christina Georgiadou, Istvan Horvath, Ludmilla A. Morozova-Roche, Philip T. F. Williamson
Summary: S100A9 is a calcium-binding protein that plays an important role in the neuroinflammatory response and development of neurodegenerative diseases. It co-aggregates with amyloid-β peptide and α-synuclein in Alzheimer's and Parkinson's diseases respectively. Calcium dyshomeostasis is known to affect S100A9's ability to adopt a fibrillar structure, but the exact mechanism is still unclear.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Chemistry, Multidisciplinary
Xingmei Qi, Yu Wang, Hairui Yu, Ruifang Liu, Axel Leppert, Zihan Zheng, Xueying Zhong, Zhen Jin, Han Wang, Xiaoli Li, Xiuzhe Wang, Michael Landreh, Ludmilla A. Morozova-Roche, Jan Johansson, Sidong Xiong, Igor Iashchishyn, Gefei Chen
Summary: Amyloid fibrils, which are highly ordered nanoscale aggregates, play a role in some incurable human diseases but also have physiological functions in nature. This study shows that spider silk proteins (spidroins) and the pathogenic amyloid-β peptide (Aβ) share amyloid-like properties but have different fibrillization pathways. Aβ forms amyloid nanofibrils through nucleation-dependent polymerization, while spidroins spontaneously and rapidly form amyloid-like nanofibrils through non-nucleation-dependent lateral packing. Spidroin nanofibrils lack cytotoxicity and do not self-seed or cross-seed human amyloidogenic peptides, suggesting that they have evolved unique primary structures to avoid the formation of cytotoxic intermediates.
Article
Multidisciplinary Sciences
Katryna Pampuscenko, Ramune Morkuniene, Lukas Krasauskas, Vytautas Smirnovas, Guy C. Brown, Vilmante Borutaite
Summary: In tauopathies, extracellular tau protein can stimulate microglia to phagocytose live neurons, leading to neuronal death via caspase-1 activation. This process is mediated by Toll-like 4 receptors, NLRP3 inflammasome, and NADPH oxidase. Inhibition of caspase-1 or suppression of NLRP3 inflammasome can prevent tau-induced neuronal loss, suggesting potential molecular targets for pharmacological treatment of tauopathies.
SCIENTIFIC REPORTS
(2023)
Article
Chemistry, Physical
N. Tan Luong, Hanna Oderstad, Michael Holmboe, Jean-Francois Boily
Summary: Water films captured in the interlayer region of birnessite nanosheets have significant impacts in various fields. The temperature-dependent loadings and properties of these films are crucial in understanding birnessite reactivity. Our study shows that birnessite intercalates one water monolayer at lower temperatures, but the loading decreases at higher temperatures. The properties of intercalated water remain unchanged, indicating the intact hydrogen bonding network. Molecular simulations suggest that the reduced water storage capacity at high temperatures is a result of evolved heat and the larger mobility of water compared to K+ ions that are bound to birnessite basal oxygens. This study sheds light on the temperature-driven intercalation of water in nanolayered minerals and provides insights for future research.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2023)
Article
Chemistry, Multidisciplinary
N. Tan Luong, Michael Holmboe, Jean-Francois Boily
Summary: Hydrophilic nanosized minerals exposed to air moisture can undergo irreversible mineralogical transformations and control chemical fluxes through thin water films. In this study, periclase nanocubes were transformed into brucite nanosheets through the nucleation-limited growth process triggered by three monolayer-thick water films. The conversion rate depended on the nanocube size and microporosity, impacting reaction yields and crystallization pressures. These findings provide new insights for understanding mineralogical transformations induced by nanometric water films and can be applied to related minerals in nature and technology.