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, Applied
Yuan Peng, Chuanyang Wang, Jian Yu, Jinhong Wu, Faxiang Wang, Yongle Liu, Xianghong Li
Summary: This study investigated the intermolecular interactions and self-assembly mechanism of rice glutelin amyloid fibril aggregates using experimental and computer simulation methods. The addition of NaCl and SDS promoted the aggregation of the fibrils, while the addition of urea caused degradation and depolymerization. Hydrogen bonding primarily drove the formation of the common cross 8-sheet structure, with hydrophobic and electrostatic interactions also involved. Molecular dynamics simulations confirmed the nucleation-elongation mechanism for the formation of the aggregates. Understanding the self-assembly pattern of amyloid fibril aggregates derived from food protein is crucial for their design and practical application.
FOOD HYDROCOLLOIDS
(2023)
Article
Chemistry, Multidisciplinary
Xingxing He, Xueqing Wang, Jifeng Liu, Shuo Wang
Summary: Controlled peptide assembly is an important method for synthesizing materials with diverse functions in polymer science. The morphology of the self-assembled heptapeptide Fmoc-AEAEAEA-CONH2 was found to be strongly influenced by experimental conditions such as temperature, pH, and solvents. The heptapeptide can form nanofibers or cubes depending on the kinetic parameters during fabrication. The rebalance of molecular interactions, such as hydrophobic interactions, hydrogen bonding, and electrostatic interactions, is responsible for the morphological conversion. The two assemblies can also function as beta-glucosidase mimics, with their catalytic activity following the density of active sites outside the assemblies.
Article
Chemistry, Multidisciplinary
Nicola Forlano, Raffaella Bucci, Alessandro Contini, Mariano Venanzi, Ernesto Placidi, Maria Luisa Gelmi, Raffaella Lettieri, Emanuela Gatto
Summary: This study describes the self-assembly properties of an alpha,beta-peptide, which can self-organize into a fascinating supramolecular rope on surfaces. The material was characterized by AFM, electronic conduction and fluorescence measurements. Molecular dynamics simulations showed that this peptide can self-assemble into an antiparallel beta-sheet layer, which can further self-assemble into many side-by-side layers. The presence of aromatic residues promoted by the alternation of alpha,beta-amino-acids in the primary sequence endorses the formation of a super-secondary structure with good electron conduction properties.
Article
Chemistry, Physical
Marta Diaz-Caballero, Susanna Navarro, Miquel Nuez-Martinez, Francesca Peccati, Luis Rodriguez-Santiago, Mariona Sodupe, Francesc Teixidor, Salvador Ventura
Summary: Researchers have designed a new type of peptide nanomaterial consisting solely of histidine and tyrosine residues, which exhibit biocompatible amyloid-like fibrils and hydrogels with hydrolytic and electrocatalytic activities. These nanofibers show controllable mesoscopic properties at different pH levels, transitioning between active beta-sheet fibrils and inactive random coil species. The structural insights derived from molecular dynamic simulations offer understanding on how these amyloid-like fibrils achieve a combination of structural and catalytic properties.
Article
Polymer Science
James P. Warren, Matthew P. Culbert, Danielle E. Miles, Steven Maude, Ruth K. Wilcox, Paul A. Beales
Summary: Self-assembling peptides are a versatile biomaterial that can form self-supporting hydrogels. Balancing attractive and repulsive forces through peptide charge and hydrogen bonding is crucial for successful hydrogel formation. A net peptide charge of +/-2 and modulating hydrogen bonding can optimize the assembly and viscoelastic properties of the hydrogel. These findings demonstrate the potential of controlling self-assembly mechanisms to create structures with desired properties.
Article
Biochemistry & Molecular Biology
Veronika Hovanova, Andrej Hovan, Gabriel Zoldak, Erik Sedlak, Martin Humenik
Summary: Recombinant spider silk proteins can be produced in large-scale fermentation processes and have proven to be valuable biomaterials for various applications. The self-assembly of these proteins into nanofibrils, which have unique properties, is essential for the creation of micro- and nanostructured scaffolds. However, understanding the molecular mechanisms behind nanofibril self-assembly remains a challenge.
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)
Review
Biochemistry & Molecular Biology
Torsten John, Lisandra L. L. Martin, Bernd Abel
Summary: This review discusses the impact of surface interfaces on the structure and aggregation mechanisms of peptides and proteins, particularly their association with amyloid fibril formation and neurodegenerative diseases. Research findings demonstrate that surface interfaces can both accelerate and inhibit peptide self-assembly, with adsorption typically promoting aggregation. The review introduces experimental and theoretical models for better understanding peptide self-assembly at hard and soft matter interfaces, and proposes relationships between biological interfaces and amyloid fibril formation.
MACROMOLECULAR BIOSCIENCE
(2023)
Article
Chemistry, Multidisciplinary
Si Sun, Hong-Wen Liang, Hao Wang, Quanming Zou
Summary: Controlled self-assembly is of great interest in biological and nanotechnological applications. We have demonstrated a light-triggered platform that allows precise control of self-assembly from nanoparticles into nanofibers in living cells. The process is biocompatible, fast, and can be applied for regulating molecular assembly in living cells.
Article
Chemistry, Applied
Jinzhao Xu, Mengqi Tang, Danping Wang, Qinggang Xie, Xiaoxi Xu
Summary: This study investigated the dynamic evolution of oat globulin (OG) fibrils during their formation, revealing that OG undergoes structural unfolding and hydrolysis before reassembling into fibrils enriched in beta-sheet structures. The formation process is driven by disulfide bonds, electrostatic, and hydrophobic interactions. Moreover, OG fibrils exhibit altered emulsifying properties and increased antioxidant function.
FOOD HYDROCOLLOIDS
(2024)
Article
Chemistry, Multidisciplinary
Susanna Navarro, Marta Diaz-Caballero, Francesca Peccati, Lorena Roldan-Martin, Mariona Sodupe, Salvador Ventura
Summary: Enzymes fold into specific 3D protein structures and exhibit high catalytic efficiency and selectivity. Artificial amyloids have been shown to have catalytic activity and advantages over natural enzymes. A recent study found that short peptides can self-assemble into amyloid fibrils with catalytic activity by coordinating and retaining different divalent metal cations. These findings provide new insights into the design of artificial metalloenzymes and support the role of amyloid-like structures in the origin of life.
Article
Chemistry, Multidisciplinary
Rong Sheng Li, Jiahui Liu, Hu Shi, Ping Ping Hu, Yao Wang, Peng Fei Gao, Jian Wang, Moye Jia, Hongwei Li, Yuan Fang Li, Chengde Mao, Na Li, Cheng Zhi Huang
Summary: Golgi apparatus-targeted nano-mechanical disruption is an attractive approach for killing cancer cells by multimodal mechanism and avoiding drug resistance. The transformable peptide C6RVRRF4KY can self-assemble into nontoxic nanoparticles in aqueous medium but transformed into left-handed helical fibrils (L-HFs) after targeting and furin cleavage in the Golgi apparatus of cancer cells, leading to mechanical disruption and death of cancer cells without acquired drug resistance. This nanomechanical disruption concept should also be applicable to multidrug-resistant bacteria and viruses.
Article
Chemistry, Multidisciplinary
Paula Mayorga-Burrezo, Carmen C. Mayorga-Martinez, Martin Pumera
Summary: Microrobots are seen as attractive mobile carriers for clinical therapies, with high expectations for their ability to navigate autonomously and perform specific tasks. In this study, self-propelled light-driven single-component micromotors based on concave BiVO4 microspheres are used to disaggregate protein fibrils by generating reactive oxygen species (ROS) on-the-fly. This promising application could potentially be extended to photodynamic therapies for conditions such as lung or skin cancer.
ADVANCED FUNCTIONAL MATERIALS
(2022)
Article
Chemistry, Applied
Jihyun Kim, Seon-Min Oh, Hui-Yun Kim, Jong-Hyun Choi, Jae-Sung Shin, Ji-Eun Bae, Sang-Jin Ye, Moo-Yeol Baik
Summary: The self-assembly kinetics of short-chain glucan aggregates prepared under isothermal conditions were investigated. The formation and crystallization rates were fastest at 4°C and 20°C. Nucleation allowed for the formation of aggregates at 60°C, and increased yield at all temperatures. All aggregates exhibited B-type crystal patterns and nanosized particles (<500 nm). Manipulation of the nucleation step is expected to be an effective method for increasing yield and producing aggregates at high temperature.
Article
Biochemistry & Molecular Biology
Emil Dandanell Agerschou, Marie P. Schuetzmann, Nikolas Reppert, Michael M. Woerdehoff, Hamed Shaykhalishahi, Alexander K. Buell, Wolfgang Hoyer
Summary: The study shows that the formation of turns in the αS protein significantly affects its fibril formation kinetics. Variants with faster beta 1'- or beta 2'-turn formation tend to aggregate more rapidly, while variants with beta 1-turn formation show slower aggregation compared to wild-type. Furthermore, turn exchanges alter fibril morphology and affect the efficiency of fibril elongation.
BIOPHYSICAL CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Anna S. Koenig, Nadine S. Roesener, Lothar Gremer, Markus Tusche, Daniel Flender, Elke Reinartz, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold, Henrike Heise
Summary: In this study, the researchers used huPrP to preserve and bind Aβ oligomers into large heteroassemblies, and investigated the conformations of Aβ(1-42) oligomers and huPrP complex using solid-state MAS NMR spectroscopy. They found that the Aβ oligomers within the complex exhibit diverse β-strand content, and not all molecules have identical conformations.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Review
Chemistry, Multidisciplinary
Dieter Willbold, Birgit Strodel, Gunnar F. Schroeder, Wolfgang Hoyer, Henrike Heise
Summary: This review focuses on the process of amyloid-type protein aggregation, discussing structures obtained from in vitro and ex vivo studies as well as a model for fibril formation. The model suggests a prion-like nature of all amyloid assemblies, but applying it to the in vivo situation remains complex and raises many unresolved issues.
Article
Multidisciplinary Sciences
Marie P. Schutzmann, Filip Hasecke, Sarah Bachmann, Mara Zielinski, Sebastian Haensch, Gunnar F. Schroeder, Hans Zempel, Wolfgang Hoyer
Summary: The formation of A beta oligomers (A beta Os) is significantly accelerated in endo-lysosomal pH conditions, leading to extensive A beta O formation under physiological conditions, which triggers Alzheimer's disease-related pathologies. Exploiting a dimeric variant of A beta, the authors demonstrate that this model construct is relevant for studying pathogenic A beta O formation and its effects on Tau missorting and impaired neuronal activity.
NATURE COMMUNICATIONS
(2021)
Article
Neurosciences
Eva M. Szego, Fabian Boss, Daniel Komnig, Charlott Gartner, Lennart Hofs, Hamed Shaykhalishahi, Michael M. M. Wordehoff, Theodora Saridaki, Jorg B. Schulz, Wolfgang Hoyer, Bjorn H. Falkenburger
Summary: The study demonstrates that AS69 can reduce alpha-synuclein pathology and associated neurodegeneration in primary neurons and in the mouse brain. AS69 was shown to interfere with fibril nucleation, reduce aggregation, and mitigate degeneration of dopaminergic axon terminals and dendrites. The findings suggest that small proteins binding the N-terminus of alpha-synuclein monomers could be a promising strategy to modify disease progression in Parkinson's disease.
FRONTIERS IN NEUROSCIENCE
(2021)
Editorial Material
Neurosciences
Claudio M. Gomes, Wolfgang Hoyer, Jinghui Luo
FRONTIERS IN NEUROSCIENCE
(2021)
Article
Chemistry, Multidisciplinary
Debabrata Maity, Yujeong Oh, Lothar Gremer, Wolfgang Hoyer, Mazin Magzoub, Andrew D. Hamilton
Summary: This study demonstrates that cucurbit[7]uril (CB[7]) can effectively inhibit the aggregation of islet amyloid polypeptide (IAPP) by interacting with the hot segments of IAPP and preventing the formation of toxic oligomers. CB[7] also protects rat insulinoma cells from cytotoxicity associated with IAPP assembly.
CHEMISTRY-A EUROPEAN JOURNAL
(2022)
Article
Multidisciplinary Sciences
Ricarda Torner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer, Jerome Boisbouvier
Summary: Integrated kinetic and structural investigations reveal that the co-chaperonin prefoldin interacts with islet amyloid polypeptide fibrils to inhibit their elongation and secondary nucleation.
NATURE COMMUNICATIONS
(2022)
Article
Biochemistry & Molecular Biology
Anne K. Braczynski, Marc Sevenich, Ian Gering, Tatsiana Kupreichyk, Emil D. Agerschou, Yannick Kronimus, Pardes Habib, Matthias Stoldt, Dieter Willbold, Jorg B. Schulz, Jan-Philipp Bach, Bjorn H. Falkenburger, Wolfgang Hoyer
Summary: Parkinson's disease is associated with changes in the abundance of naturally occurring antibodies (nAbs) against alpha-synuclein (α Syn). In this study, nAbs-alpha Syn were found to specifically bind monomeric α Syn and inhibit its aggregation in vitro. Additionally, the addition of nAbs-alpha Syn to cultured cells affected intracellular α Syn aggregates.
Editorial Material
Chemistry, Multidisciplinary
Debabrata Maity, Yujeong Oh, Lothar Gremer, Wolfgang Hoyer, Mazin Magzoub, Andrew D. Hamilton
CHEMISTRY-A EUROPEAN JOURNAL
(2022)
Article
Biochemistry & Molecular Biology
Yue Lu, Zsuzsanna Voros, Gustavo Borjas, Cristin Hendrickson, Keith Shearwin, David Dunlap, Laura Finzi
Summary: DNA can act as a scaffold for the cooperative binding of protein oligomers. The structure formed by phage 186 CI and lambda CI repressors do not significantly interfere with transcription.
Article
Medicine, General & Internal
Marlene Pils, Alexandra Dybala, Fabian Rehn, Lara Bloemeke, Tuyen Bujnicki, Victoria Kraemer-Schulien, Wolfgang Hoyer, Detlev Riesner, Dieter Willbold, Oliver Bannach
Summary: Protein misfolding and aggregation are key factors in neurodegenerative diseases. In this study, a synthetic β-amyloid oligomer sample was developed for quality control and standardization of diagnostic methods. The combination of atomic force microscopy and fluorescence analysis showed promising results for the detection of Aβ oligomers in bodily fluids.
Article
Biochemistry & Molecular Biology
Laetitia F. Heid, Tatsiana Kupreichyk, Marie P. Schuetzmann, Walfried Schneider, Matthias Stoldt, Wolfgang Hoyer
Summary: Heterologous interactions between different amyloid-forming proteins can have a significant impact on disease-related amyloid formation. In this study, researchers tested how heterologous beta-hairpins derived from immunoglobulin light chains modulate the fibril formation of Parkinson's disease-associated protein alpha-synuclein. They found that the addition of these beta-hairpins affects the kinetics of alpha-synuclein aggregation, suggesting they support the nucleation of amyloid fibrils.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
