Article
Neurosciences
Peizhou Jiang, Ming Gan, Dennis W. Dickson
Summary: This study demonstrates that nuclear extracts from apoptotic cells can induce intracellular alpha S aggregation in susceptible cells, suggesting a contribution of histone amyloid fibrils to alpha S aggregation. Additionally, recombinant histone-derived amyloid fibrils are able to induce alpha S aggregation in cellular and animal models, and this effect is associated with lysosome rupture mediated by endocytosis.
MOLECULAR NEUROBIOLOGY
(2021)
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
Qichen Pan, Yunchao Ban, Suliman Khan
Summary: The study demonstrated that calycosin significantly inhibits the fibril formation of α-syn in a concentration-dependent manner, preventing α-syn amyloid-triggered neurotoxicity. By modifying the aggregation pathway, calycosin promotes the formation of non-toxic species, restoring SOD/CAT activity and GSH content while reducing ROS levels and caspase-3 activity. This research provides valuable insights into the mechanism of α-syn amyloid inhibition by calycosin and suggests the development of small molecules-based therapeutic platforms for Parkinson's disease.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Neurosciences
Rebecca J. Thrush, Devkee M. Vadukul, Francesco A. Aprile
Summary: This study presents a method to generate N-terminally truncated variants of alpha-synuclein without extra terminal residues. It has been determined that the first six residues of this protein play an important role in the formation of amyloids.
FRONTIERS IN NEUROSCIENCE
(2022)
Article
Biochemistry & Molecular Biology
Ramin Zadali, Vahid Hassani, Yasin Rafiei, Ali Akbar Meratan, Fatemeh Mamashli, Mohsen Nemat-Gorgani
Summary: The study investigated the effects of amyloid fibrils from alpha-syn and HEWL on rat brain and liver mitochondria, showing that alpha-syn fibrils exhibited more toxicity compared to HEWL. Both types of fibrils were found to induce toxicity in SH-SY5Y cells and erythrocytes.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
(2022)
Review
Biochemistry & Molecular Biology
Parveen Salahuddin, Munazza Tamkeen Fatima, Vladimir N. Uversky, Rizwan Hasan Khan, Zeyaul Islam, Mohammad Furkan
Summary: Neurodegenerative diseases are characterized by the abnormal loss of neurons, with common pathogenic mechanisms involving misfolding and aggregation of proteins. Accumulating evidence suggests that amyloid oligomers, not fibrils, are the most toxic species causing AD and PD.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Review
Biochemistry & Molecular Biology
Surabhi Mehra, Laxmikant Gadhe, Riya Bera, Ajay Singh Sawner, Samir K. Maji
Summary: Abnormal accumulation of aggregated alpha-synuclein is a common feature in various neurodegenerative diseases, exhibiting clinical and pathological differences similar to prion disorders. Emerging evidence suggests that alpha-Syn self-assembles into conformationally diverse polymorphs, which may contribute to the clinical heterogeneity in synucleinopathies.
Article
Chemistry, Multidisciplinary
Shengnan Zhang, Juan Li, Qianhui Xu, Wencheng Xia, Youqi Tao, Chaowei Shi, Dan Li, ShengQi Xiang, Cong Liu
Summary: Many amyloid fibrils associated with neurodegenerative diseases consist of an ordered fibril core and disordered terminal regions. In this study, we used solid-state NMR and cryo-EM techniques to explore the intact structure of an alpha-syn fibril and studied its conformational dynamics upon binding to the LAG3 receptor. Our findings reveal the synergistic conformational transition of the intrinsically disordered terminal regions of alpha-syn, shedding light on the role of these regions in regulating amyloid fibril structure and pathology.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Biochemistry & Molecular Biology
Lisni P. Sunny, Priya Srikanth, Anju Kunhiraman Sunitha, Niyoti Tembulkar, Jancy Nixon Abraham
Summary: This study discusses the interactions of novel tryptophan-cardanol nanoparticles with alpha-synuclein protein monomers and fibrils, showing that these nanoparticles can effectively disrupt alpha-synuclein fibrils and inhibit their formation, as well as disassemble amyloid fibrils, indicating potential therapeutic benefits for synucleinopathies.
JOURNAL OF PEPTIDE SCIENCE
(2022)
Article
Multidisciplinary Sciences
Roberta Cascella, Serene W. Chen, Alessandra Bigi, Jose D. Camino, Catherine K. Xu, Christopher M. Dobson, Fabrizio Chiti, Nunilo Cremades, Cristina Cecchi
Summary: The self-assembly of alpha-synuclein (alpha S) is a pathological feature of Parkinson's disease. The authors demonstrate that alpha S fibrils release soluble prefibrillar oligomeric species responsible for neurotoxicity in vitro.
NATURE COMMUNICATIONS
(2021)
Review
Chemistry, Multidisciplinary
Yuxing Ma, Xiaofang Li, Ruoyang Zhao, Enqi Wu, Qiqige Du, Jun Guo, Liping Wang, Feng Zhang
Summary: DNA origami and protein origami can both create complex artificial nanostructures, but protein origami has an advantage in terms of versatility due to the limited number of nucleotides. Despite the similarities between peptides and DNA in structure and properties, using peptides instead of DNA to create complex bioactivities is still a challenge.
Article
Biochemistry & Molecular Biology
Jan Gombos, Lucia Balejcikova, Peter Kopcansky, Marianna Batkova, Katarina Siposova, Jozef Kovac, Kristina Zolochevska, Ivo Safarik, Alica Lokajova, Vasil M. Garamus, Dusan Dobrota, Oliver Strbak
Summary: This article investigates the destructive effect of ferritin derivatives on lysosome amyloid fibrils and the release of iron ions. The results suggest that ferritin derivatives have both therapeutic and adverse effects, which may play a significant role in future biomedical applications.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
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
Biochemistry & Molecular Biology
Yasin Rafiei, Bahram Salmani, Behnaz Mirzaei-Behbahani, Mahshid Taleb, Ali Akbar Meratan, Mohammad Ramezani, Nasser Nikfarjam, Stefan Becker, Nasrollah Rezaei-Ghaleh
Summary: Natural compound PFP nanosheets inhibit the amyloid aggregation of α-synuclein and redirect its aggregation towards nontoxic off-pathway oligomers. The binding of PFP nanosheets with α-synuclein amyloid fibrils demonstrates their potential anti-aggregation activity in neurodegenerative diseases.
ACS CHEMICAL NEUROSCIENCE
(2022)
Article
Biochemistry & Molecular Biology
John R. Horsley, Blagojce Jovcevski, Tara L. Pukala, Andrew D. Abell
Summary: This study demonstrates the effectiveness of using D-peptide inhibitors targeting the NTR region of α-synuclein (α S) to prevent aggregation and fibril formation, and reduce the cytotoxicity of α S aggregates. This approach provides a potential strategy for treating Parkinson's disease.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2022)