Article
Chemistry, Physical
Moe Yamazaki, Keisuke Ikeda, Tomoshi Kameda, Hiroyuki Nakao, Minoru Nakano
Summary: This study investigates the kinetic mechanism of amyloid fibril formation by a peptide fragment containing seven residues of the amyloid-beta protein Aβ-(16-22). The results show that the unprotected peptide fragment can rapidly form fibrils in a neutral aqueous buffer solution, and the fibrillation kinetics can be described by the nucleation-elongation model. The width of the fibrils increases over time, possibly due to lateral association. Electrostatic and hydrophobic interactions play important roles in the fibrillation process.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2022)
Article
Biotechnology & Applied Microbiology
Theyencheri Narayanan, Axel Ruter, Ulf Olsson
Summary: This brief report presents an X-ray scattering investigation of self-assembled nanotubes formed by a short peptide, demonstrating the quantitative determination of nanotube dimensions and crystalline organization within their walls, using amyloid-beta(16-22) peptide nanotubes as an illustrative example.
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Nan Yuan, Lianmeng Ye, Yan Sun, Hao Wu, Zhengpan Xiao, Wanmeng Fu, Zuqian Chen, Yechun Pei, Yi Min, Dayong Wang
Summary: The major pathological feature of Alzheimer's disease (AD) is the aggregation of amyloid beta peptide (A beta) in the brain. Inhibition of A beta(42) aggregation may prevent the advancement of AD. This study found that arginine dipeptide (RR) was the most effective at interfering with A beta(42) polymerization and reducing its toxicity, including cell death, reactive oxygen species (ROS) production, and apoptosis.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Yang Gao, Stefan Wennmalm, Bengt Winblad, Sophia Schedin-Weiss, Lars O. Tjernberg
Summary: Through FRET imaging, Aβ42 oligomerization was successfully detected in primary neurons, showing that Aβ42 oligomerized in lysosomes/late endosomes in a concentration-dependent manner. These findings contribute to a better understanding of Aβ42 oligomerization in neurons.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Chemistry, Multidisciplinary
Peter Faller, Christelle Hureau
Summary: Controlling protein and peptide aggregation in vitro and obtaining reproducible results poses a challenge, which is scarcely reported and discussed in the literature, potentially hindering progress in the field and misleading newcomers.
FRONTIERS IN CHEMISTRY
(2021)
Review
Biochemistry & Molecular Biology
Satoru Itoh, Hisashi Okumura
Summary: Aggregates of amyloid-beta (Aβ) peptides are enhanced at hydrophilic-hydrophobic interfaces and inhibited by polyphenols. Aβ40 accelerates aggregation due to its beta-hairpin structure, while polyphenols inhibit Aβ(16-22) aggregation by forming hydrogen bonds.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Sara La Manna, Daniele Florio, Ilaria Iacobucci, Fabiana Napolitano, Ilaria De Benedictis, Anna Maria Malfitano, Maria Monti, Mauro Ravera, Elisabetta Gabano, Daniela Marasco
Summary: The effects of three platinum complexes on the aggregation of an amyloid model system were investigated, showing the ability of these compounds to repress amyloid aggregation and interact with the ligand field of Aβ peptide. Spectroscopic data and circular dichroism studies revealed that Pt-terpy induces soluble β-structures of monomeric Aβ(21-40) and reduces self-recognition, ultimately reducing cytotoxicity in human neuroblastoma cells. These findings suggest the potential application of metal-based agents as neurodrugs for neurodegenerative diseases.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Chemistry, Physical
Xuan Tang, Wei Han
Summary: This study develops a multiscale approach to explore the pathways and kinetics of peptide aggregation nucleation. The research reveals a two-step mechanism for A beta(16-21) amyloid nucleation, and an unexpected atypical mechanism at submillimolar concentrations.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2022)
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, Multidisciplinary
Milad Zangiabadi, Avijit Ghosh, Yan Zhao
Summary: The aggregation of Aβ peptides in Alzheimer's disease involves complex interactions between hydrophobic and polar residues. Molecularly imprinted nanoparticle (MINP) receptors strongly bind specific segments of Aβ(40), inhibiting the aggregation of monomeric A040 through binding residues 21-30 near the loop region. Residues 11-20, including the internal 0 strand closer to the N-terminal, represent the best target for disaggregating already formed aggregates during the polymerization phase. Binding residues 1-10 have the greatest effect on disaggregation in the saturation phase.
Article
Chemistry, Physical
Jiuhong Zhao, Na Xu, Xiaotong Yang, Guixia Ling, Peng Zhang
Summary: Alzheimer's disease is the most common form of dementia in humans, and it is related to the misfolding and aggregation of Aβ peptides. Gold nanoparticles have excellent properties and can be used in the diagnosis and drug delivery for AD.
COLLOID AND INTERFACE SCIENCE COMMUNICATIONS
(2022)
Article
Biochemistry & Molecular Biology
Mark M. Stecker, Ankita Srivastava, Allison B. Reiss
Summary: This study used an in vitro rat sciatic nerve model to investigate the effects of A beta 42 on the nervous system. The results showed that A beta 42 primarily reduces the amplitude of the nerve action potential, and this effect is significantly concentration-dependent.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Mueed Ur Rahman, Kaiyuan Song, Lin-Tai Da, Hai-Feng Chen
Summary: By using molecular dynamics simulations and Markov state model, the early oligomerization mechanism of A beta(16-22) peptides was investigated. It was found that the dimeric form of the peptides adopted globular random-coil or extended beta-strand like conformations, and intermolecular antiparallel beta-sheets were the most common type of secondary structure in the observed dimers. The states containing beta secondary structure and extended coiled structures were majorly involved in aggregation.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biochemistry & Molecular Biology
Daniela Marasco, Caterina Vicidomini, Pawel Krupa, Federica Cioffi, Pham Dinh Quoc Huy, Mai Suan Li, Daniele Florio, Kerensa Broersen, Maria Francesca De Pandis, Giovanni N. Roviello
Summary: Different isoquinoline alkaloids exhibit varying effects on beta-amyloid aggregation, with some compounds showing inhibitory effects and others showing promoting effects. Experimental results suggest that these compounds have the potential to serve as starting leads for the development of therapeutic strategies in neurodegenerative diseases.
CHEMICO-BIOLOGICAL INTERACTIONS
(2021)
Article
Cell Biology
Jacopo Lesma, Faustine Bizet, Corentin Berardet, Nicolo Tonali, Sara Pellegrino, Myriam Taverna, Lucie Khemtemourian, Jean-Louis Soulier, Carine van Heijenoort, Frederic Halgand, Tap Ha-Duong, Julia Kaffy, Sandrine Ongeri
Summary: This study focuses on designing and synthesizing new compounds to inhibit hIAPP aggregation, and biophysical evaluations demonstrate that these compounds effectively inhibit the aggregation process of hIAPP.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2021)
Article
Multidisciplinary Sciences
Mara Chiricotto, Fabio Sterpone, Philippe Derreumaux, Simone Melchionna
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES
(2016)
Article
Chemistry, Physical
Mara Chiricotto, Fausto Martelli, Giuliana Giunta, Paola Carbone
Summary: The wetting behavior of graphitic surface-water interfaces was studied through detailed atomistic molecular dynamics simulations, revealing that wetting is determined by a fine balance between van der Waals and electrostatic interactions. The presence of vacuum and the hydrophobic nature of graphene influence the rearrangement of water molecules near the surface, impacting the hydrogen bond network and surface tension. The number of graphene layers affects the topology of the hydrogen bond network and stability, influencing the wettability of various graphene configurations.
JOURNAL OF PHYSICAL CHEMISTRY C
(2021)
Article
Physics, Condensed Matter
G. Giunta, M. Chiricotto, I Jackson, H. A. Karimi-Varzaneh, P. Carbone
Summary: The dispersion of inorganic particles within polymeric materials is a widely used method to enhance mechanical properties. Modeling the uneven surface of fillers in polymer composites is a major challenge, which affects the dynamics of adsorbed polymers and the mechanical properties of the final composite. A new multiscale approach using experimental data is proposed to statistically reproduce surface defects and analyze the structure and dynamics of polymer chains in contact with different carbon black samples. The heterogeneous surface has a negligible influence on polymer chain structure but a major effect on their dynamics and surface wettability.
JOURNAL OF PHYSICS-CONDENSED MATTER
(2021)
Article
Chemistry, Physical
Zixuan Wei, Mara Chiricotto, Joshua D. Elliott, Fausto Martelli, Paola Carbone
Summary: In this study, the behavior of water in graphite nanoslits was simulated using molecular dynamics. It was found that graphite is more hydrophobic in the nanoslit than in bulk. The study also revealed that the value of interfacial tension oscillates and eventually converges to a constant value within a certain range of nanochannel heights. Furthermore, a critical channel height was identified, at which the surface tension reaches its maximum value while water diffusion across the channel is at its minimum. These findings have important implications for understanding the thermodynamics of solid/liquid interfaces and interpreting experimental permeability data.