Article
Biochemistry & Molecular Biology
Jekabs Fridmanis, Zigmantas Toleikis, Tomas Sneideris, Mantas Ziaunys, Raitis Bobrovs, Vytautas Smirnovas, Kristaps Jaudzems
Summary: Researchers have successfully developed structural models of mouse prion protein fibrils prepared under three different denaturing conditions using atomic force microscopy, FTIR spectroscopy, and magic-angle spinning NMR. The study revealed that while the core region and N- and C-terminal structures are almost identical among the three fibrils, the central part differs in terms of beta-strand length and charged residue arrangement. This suggests that the ionic strength of the denaturant plays a key role in determining the structure of fibrils under specific conditions.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Agriculture, Dairy & Animal Science
Almut H. Vollmer, Ingrun Kieferle, Alexandra Pusl, Ulrich Kulozik
Summary: The study revealed that varying the concentration of pentasodium triphosphate had significant effects on the rheological, textural, and microstructural properties of processed cheese, with higher concentrations of PP leading to increased apparent viscosity, hardness, and the formation of casein fibrils.
JOURNAL OF DAIRY SCIENCE
(2021)
Article
Biochemistry & Molecular Biology
Daniel Kachkin, Kirill V. Volkov, Julia Sopova, Alexander G. Bobylev, Sergei A. Fedotov, Sergei G. Inge-Vechtomov, Oxana Galzitskaya, Yury O. Chernoff, Aleksandr A. Rubel, Anna Y. Aksenova
Summary: This study assessed the amyloid properties of RAD51 protein in vitro and in a bacterial system. The purified human RAD51 protein formed amyloid-like aggregates with a cross-beta fibrillar structure, and were stained with amyloid-specific dyes. Cytoplasmic aggregates of RAD51 were also observed in cell cultures overexpressing RAD51.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Nanoscience & Nanotechnology
Bole Li, Chang Xu, Yanfei Lv, Guihao Liu, Xiaoliang Sun, Zeqian Sun, Xiaotong Xu, Wei Chen, Lei He, Yu-Fei Song
Summary: In this study, vanadium-substituted tungsten and molybdenum POMs (W- and Mo-POMs) were used to oxidize PrP106-126 protein. W-POMs showed higher structural stability and stronger binding and oxidation effects on PrP compared to Mo-POMs. The substitution of W/Mo by vanadium enhanced the hydrogen bonding with the histidine site. PW10V2 exhibited the strongest oxidation on the methionine residue of PrP, resulting in excellent inhibition of PrP aggregation and significant attenuation of its neurotoxicity.
ACS APPLIED MATERIALS & INTERFACES
(2023)
Article
Biochemistry & Molecular Biology
Tomasz Zajkowski, Michael D. Lee, Shamba S. Mondal, Amanda Carbajal, Robert Dec, Patrick D. Brennock, Radoslaw W. Piast, Jessica E. Snyder, Nicholas B. Bense, Wojciech Dzwolak, Daniel F. Jarosz, Lynn J. Rothschild
Summary: The discovery of functional prion-forming domains in archaea expands our knowledge of prions to the third domain of life, suggesting they may have existed at the time of the last universal common ancestor. This study provides evidence that multiple archaeal proteins can act as prions, driving non-Mendelian patterns of inheritance by forming amyloids. The higher tyrosine and phenylalanine content in positively tested candidates may aid in future predictions of archaeal prions.
MOLECULAR BIOLOGY AND EVOLUTION
(2021)
Article
Chemistry, Multidisciplinary
Yoshitake Sakae, Takeshi Kawasaki, Yuko Okamoto
Summary: This study focused on the concentration dependency of fibril-forming peptides, showing that density fluctuation, beta-structures, and oligomers of KFFE fragments increased in high concentration environments, indicating a likelihood of protein aggregation.
Article
Food Science & Technology
Zhiming Wang, Yuanyuan Deng, Yan Zhang, Zhencheng Wei, Zhili Wan, Chao Li, Xiaojun Tang, Zhihao Zhao, Pengfei Zhou, Ping Li, Guang Liu, Mingwei Zhang
Summary: The gelation of whey protein fibrils (WFs) is influenced by the protein conformation, which can be affected by citric acid (CA) and pH. This study investigated the effects of CA concentration and pH on the gelation mechanism and rheological properties of WFs hydrogels. The results showed that CA promoted hydrophobic interactions and facilitated hydrogen bond formation at acidic condition, while induced covalent cross-linking at non-acidic condition. However, excessive cross-linking was detrimental to gel formation. Despite the differences in gelation mechanism, the three types of WFs hydrogels exhibited similar physical changes and mouthfeel during oral processing.
LWT-FOOD SCIENCE AND TECHNOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Kaori Tsukakoshi, Rikako Kubo, Kazunori Ikebukuro
Summary: In this study, a fusion protein called PrP-ALP was developed as a sensing element to detect toxic A beta oligomers. PrP-ALP showed strong affinity towards high molecular weight oligomers and has potential for detecting A beta oligomers. This study is important for understanding the pathogenesis of Alzheimer's disease.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biology
Haruka Narita, Tomohiro Shima, Ryo Iizuka, Sotaro Uemura
Summary: The N-terminal region of Argonaute2 can form amyloid-like aggregates, which may regulate the RNA silencing activity of DmAgo2.
Article
Chemistry, Multidisciplinary
Jiangtao Zhou, Ting Li, Mohammad Peydayesh, Mattia Usuelli, Viviane Lutz-Bueno, Jie Teng, Li Wang, Raffaele Mezzenga
Summary: Amyloid functional materials derived from oat globulin show diverse functionalities with rich polymorphism, reversible and irreversible fibrillization processes. These materials can be applied in water purification, sensors, and electrodes, with demonstrated sustainability against other protein sources for environmentally-efficient advanced materials and technologies.
Article
Biochemistry & Molecular Biology
Bjorn Johansson, Sho Oasa, Aida Muntsant Soria, Ann Tiiman, Linda Soderberg, Ebba Amandius, Christer Moller, Lars Lannfelt, Lars Terenius, Lydia Gimenez-Llort, Vladana Vukojevic
Summary: Traditional fluorescence microscopy has limited spatial resolution, while electron microscopy lacks molecular specificity and has limited field of view. The use of STED microscopy with fluorescently labeled antibodies enables visualization of amyloidogenic aggregates with sub-diffraction limited spatial resolution. This advancement is crucial for understanding the etiology of Alzheimer's disease and developing anti-amyloid treatments.
CELL AND BIOSCIENCE
(2023)
Article
Biology
Cristina Batlle, Isabel Calvo, Valentin Iglesias, Cian J. Lynch, Marcos Gil-Garcia, Manuel Serrano, Salvador Ventura
Summary: Recent evidence suggests that coiled-coil (CC) regions overlapping with polyQ tracts play a critical role in amyloid formation and functional switch in human proteins. The human MED15 Mediator complex subunit forms homodimers in solution mediated by CC interactions, with MED15CC aggregating into amyloid fibrils.
COMMUNICATIONS BIOLOGY
(2021)
Article
Chemistry, Multidisciplinary
Evelyn Rose Kamski-Hennekam, Jinfeng Huang, Rashik Ahmed, Giuseppe Melacini
Summary: The ability of ATP to modulate protein solubility is critical in understanding proteinopathies like Parkinson's disease. ATP levels decline with age, which is the most significant risk factor for Parkinson's. This study shows that ATP affects multiple stages of alpha-synuclein aggregation, and the disruption of ATP's function may play a role in Parkinson's etiology.
Review
Biochemistry & Molecular Biology
Anna Sulatskaya, Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail Belousov, Kirill S. Antonets, Maksim Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya Stepanenko, Anton A. Nizhnikov
Summary: Both amyloids and beta-barrel proteins have beta-sheet-rich structures, with the latter being able to form functional amyloids in vivo. These beta-barrel amyloid proteins can interact with each other and form toxic oligomers, potentially contributing to the development of amyloidoses. Rapidly growing discoveries suggest that the number and diversity of functions of amyloid-forming beta-barrel proteins are significantly greater than currently understood.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Chemistry, Physical
Adolfo B. Poma, Tran Thi Minh Thu, Lam Tang Minh Tri, Hoang Linh Nguyen, Mai Suan Li
Summary: Alzheimer's disease is a neurodegenerative disorder associated with A beta peptide aggregation. Recent experiments suggest that oligomers are more toxic than mature fibrils, leading researchers to investigate factors that may influence the properties of oligomers.
JOURNAL OF PHYSICAL CHEMISTRY B
(2021)
Article
Neurosciences
Katryna Pampuscenko, Ramune Morkuniene, Lukas Krasauskas, Vytautas Smirnovas, Taisuke Tomita, Vilmante Borutaite
Summary: Recent experimental models have shown a link between extracellular tau and neurodegeneration, but the exact mechanisms by which extracellular tau induces neuronal death remain unclear. This study found that extracellular phosphorylated tau(2N4R) is the most toxic form, causing neuronal loss at low nanomolar concentrations, and the neurotoxicity of tau(1N4R) depends on its aggregation state.
MOLECULAR NEUROBIOLOGY
(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, Physical
S. Strazdaite, S. J. Roeters, A. Sakalauskas, T. Sneideris, J. Kirschner, K. B. Pedersen, B. Schiott, F. Jensen, T. Weidner, V Smirnovas, G. Niaura
Summary: The study investigated the interactions between model lipid monolayers and Aβ in different states using surface-sensitive vibrational sum-frequency generation (VSFG) spectroscopy. The results showed that the interaction between Aβ aggregates and lipid monolayers depended on the structure of the aggregates and the type of lipid layer, with a correlation between the amide-II' signal and the degree of amyloid aggregates.
JOURNAL OF PHYSICAL CHEMISTRY B
(2021)
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
Biochemistry & Molecular Biology
Kamile Mikalauskaite, Mantas Ziaunys, Vytautas Smirnovas
Summary: This study examines the impact of the initial folding state of a protein on amyloid fibril formation, revealing a correlation between protein state and the kinetics and structural properties of the resulting fibrils.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
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
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
Multidisciplinary Sciences
Mantas Ziaunys, Andrius Sakalauskas, Kamile Mikalauskaite, Vytautas Smirnovas
Summary: Protein aggregation in the form of amyloid fibrils is associated with the development of various neurodegenerative disorders. Despite extensive research, the process of aggregate formation is not fully understood. It has been observed that α-synuclein and amyloid beta aggregates can undergo structural rearrangements after long-term incubation. This study investigates the impact of elevated temperature on the restructuring of four different conformation α-synuclein amyloid fibrils, and demonstrates that this structural alteration occurs within a relatively short period of time.
Article
Biochemistry & Molecular Biology
Andrius Sakalauskas, Agne Janoniene, Gediminas Zvinys, Kamile Mikalauskaite, Mantas Ziaunys, Vytautas Smirnovas
Summary: Research has found that the autoxidation products of flavone have inhibitory effects on amyloid-beta and alpha-synuclein aggregation, and can reduce their toxicity to cells.
Article
Biochemistry & Molecular Biology
Mantas Ziaunys, Vytautas Smirnovas
Summary: Aggregation of amyloidogenic proteins/peptides is associated with amyloid-related disorders, but effective treatments are limited. Recent studies have focused on naturally occurring molecules as potential anti-aggregation compounds, with promising results for EGCG. However, the stability of EGCG under physiological conditions is limited, and its autoxidation products may be the actual inhibitory compounds. This study investigates the association of different EGCG autoxidation products with non-aggregated insulin and their effects on aggregation and fibril structure, revealing a specific incubation time that affects the amyloid aggregation process.
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
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
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)