Article
Chemistry, Multidisciplinary
Yangyang Han, Yiping Cao, Jiangtao Zhou, Yang Yao, Xiaodong Wu, Sreenath Bolisetty, Michael Diener, Stephan Handschin, Canhui Lu, Raffaele Mezzenga
Summary: A facile and general method for fabricating amyloid films via electrostatic self-assembly is introduced, allowing for the construction of multifunctional films and smart devices. The films exhibit tunable properties and have been successfully used in the preparation of a magnetically oriented soft robotic swimmer and a smart magnetic sensor.
Review
Chemistry, Inorganic & Nuclear
Jong -Min Suh, Mingeun Kim, Jeasang Yoo, Jiyeon Han, Cinthya Paulina, Mi Hee Lim
Summary: The aggregation and accumulation of amyloidogenic peptides and proteins in the brain are pathological features of neurodegenerative disorders. Metal ions play a role in their aggregation and cytotoxicity through direct and indirect interactions. Understanding these interactions can help us understand the complicated nature of neurodegenerative diseases and develop effective diagnostics and therapeutics.
COORDINATION CHEMISTRY REVIEWS
(2023)
Article
Chemistry, Physical
Nico Kummer, Caroline E. Giacomin, Peter Fischer, Silvia Campioni, Gustav Nystrom
Summary: Amyloid fibrils from inexpensive food proteins and nanocellulose have diverse applications and their hybrid materials have improved mechanical properties due to electrostatic interactions. These interactions increase the elasticity of the amyloid network by cross-linking individual fibrils. The combination of nanocellulose morphology contributes differently to the elasticity, with cellulose nanocrystals inducing bundling and network formation, and cellulose nanofibrils forming a second network. The gained knowledge on colloidal interactions provides a basis for designing functional biohybrid materials.
JOURNAL OF COLLOID AND INTERFACE SCIENCE
(2023)
Article
Chemistry, Multidisciplinary
Zhongju Ye, Zhao-Jun Yan, Chenhong Zhang, Jun-Li Hou, Shijing Yue, Lehui Xiao
Summary: Anti-A beta therapy has been the main focus in clinical trials for AD prevention and treatment. This study introduced a new strategy using a charged tubular supramolecule to suppress A beta fibrillation, showing efficient inhibition of A beta(40) fibrillation by CTS-A at a very low inhibitor:peptide molar ratio (1:10) and a reduced cytotoxic effect of A beta peptides post-inhibition or disaggregation. The organized supramolecular structure enhances amyloid fibrillar modulation, offering a new approach for AD treatment using supramolecules.
Review
Pharmacology & Pharmacy
Jenat Pazheparambil Jerom, Sooryalekshmi Madhukumar, Raveendran Harikumaran Nair, Sunilkumar Puthenpurackal Narayanan
Summary: Molecular self-assembly is used for applications such as hydrogel preparation, tissue repair, and therapeutic drug delivery. However, self-assembly of amino acids, peptides, and proteins can lead to disorders. This review provides information on phytochemicals that can prevent or destabilize self-assemblies.
DRUG DISCOVERY TODAY
(2023)
Article
Biophysics
Shaopei Li, Kagan Kerman
Summary: Electrochemical biosensors have been utilized in studying biometal-protein interactions in neurodegenerative diseases such as Alzheimer's and Parkinson's. These sensors have shown promise in monitoring conformational changes induced by biometals and identifying disease biomarkers like amyloid-beta and alpha-synuclein.
BIOSENSORS & BIOELECTRONICS
(2021)
Review
Cell Biology
Mario Gonzalez-Garcia, Giuliana Fusco, Alfonso De Simone
Summary: The conversion of soluble proteins into insoluble amyloid aggregates is linked to various neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. The small prefibrillar oligomers formed during protein aggregation are identified as the most harmful species. Interactions with biological membranes play a crucial role in the onset of cellular toxicity. Further research is needed to understand the transient interactions involving heterogeneous protein aggregates for developing effective therapeutic strategies against protein misfolding diseases.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Zeyaul Islam, Mohamed H. Ali, Anton Popelka, Raghvendra Mall, Ehsan Ullah, Janarthanan Ponraj, Prasanna R. Kolatkar
Summary: Amyloid fibrillation, related to various neurological disorders, was studied by examining lysozyme fibrillation using nano-infrared spectroscopy (nanoIR). The study showed that lysozyme transformed into mainly parallel beta-sheets in its fibrillar structure, and nanoIR can complement other biophysical studies in analyzing the aggregation process for potential therapeutic design against amyloid disorders.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2021)
Article
Biochemistry & Molecular Biology
Seerat Siraj, Daraksha Yameen, Shivani Bhati, Teeba Athar, Salman Khan, Jaydeep Bhattacharya, Asimul Islam, Mohammad Mahfuzul Haque
Summary: Mechanisms of protein aggregation are important in therapeutic biology and neurodegenerative medicine. Macromolecular crowding affects the diffusion and folding of proteins and can cause aggregation, leading to neurodegenerative disorders and amyloidosis. Glucose has been found to prevent fibrillation and provide stability to proteins.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Li Li, Wan-Chun Luo, Ming Jiang, Xu Yu, Li Xu
Summary: The aggregation of amyloid proteins is closely related to neurodegenerative and metabolic diseases. Detecting amyloid fibrils is essential for understanding the diseases and advancing drug discovery and treatment. In this study, three proto-berberine alkaloids were examined as fluorescent probes for detecting amyloid fibrils. These alkaloids exhibited sensitivity to viscosity and polarity, enabling them to probe insulin and lysozyme fibrils with turn-on fluorescence without interfering with the fibrillation process. They also successfully monitored the aggregation process of amyloid proteins in vitro and imaged the fibrils in living cells, showing their potential as candidate fluorescent probes for amyloid fibrils.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Chemistry, Multidisciplinary
Cagla Sahin, Aikaterini Motso, Xinyu Gu, Hannes Feyrer, Dilraj Lama, Tina Arndt, Anna Rising, Genis Valentin Gese, B. Martin Haellberg, Erik. G. Marklund, Nicholas P. Schafer, Katja Petzold, Kaare Teilum, Peter G. Wolynes, Michael Landreh
Summary: Liquid-liquid phase separation (LLPS) of heterogeneous ribonucleoproteins (hnRNPs) was studied using protein engineering, native ion mobility mass spectrometry, and molecular dynamics simulations. The experiments focused on hnRNPs FUS, TDP-43, and hCPEB3 involved in neurodegeneration, cancer, and memory storage. Conformational changes associated with LLPS were monitored by releasing the proteins inside the mass spectrometer from their native assemblies. The results revealed different assembly mechanisms and potentially different impacts on RNA processing and translation depending on the protein species.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(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
Nanoscience & Nanotechnology
Yujuan Cao, Zhenyan He, Yuting Gao, Yanru Xin, Liang Luo, Fanling Meng
Summary: In this study, a bait-hook-devastate strategy was developed to improve the efficiency of photodynamic degradation of amyloid aggregates by utilizing electronic interactions to accumulate aggregates and photosensitizer in a confined area. The strategy significantly enhanced the utilization rate of generated ROS and ability to dissociate the aggregates, resulting in rapid and complete degradation of amyloid aggregates under mild conditions. This new paradigm offers a potential solution for accelerating photodynamic degradation of amyloid aggregates for practical applications.
ACS APPLIED MATERIALS & INTERFACES
(2021)
Review
Biochemistry & Molecular Biology
Diane L. Ritchie, Marcelo A. Barria
Summary: Accumulation and propagation of misfolded proteins in the brain are shared pathological features of many neurodegenerative diseases. While there is no epidemiological evidence suggesting infectiousness in neurodegenerative disorders, experimental models show potential prion-like transmission of other pathogenic proteins. Concerns exist regarding the transmission of misfolded proteins beyond prion protein.
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.