Article
Biochemistry & Molecular Biology
Fatima Kamal Zaidi, Rajiv Bhat
Summary: This study investigates the influence of curcumin and EGCG on the amyloid fibril formation of human lysozyme (HuL) and explores the mechanisms of their action. Curcumin inhibits HuL fibrillation by interacting with prefibrillar and fibrillar intermediates, while also disaggregating preformed fibrils. On the other hand, EGCG suppresses fibrillation but modulates the pathway towards large, β-sheet rich amyloid fibril-like aggregates and modifies preformed fibrils. Despite forming large agglomerates, both curcumin and EGCG reduce the surface hydrophobicity and cytotoxicity of HuL, possibly due to the dense and highly clustered nature of the aggregates.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2022)
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
Engineering, Chemical
Ying-Chu Wang, You-Ren Lai, Josephine W. Wu, Steven S. -S. Wang, Kuen-Song Lin
Summary: The study investigated the catalytic performance of palladium nanoparticles-deposited onto lysozyme amyloid fibrils, finding that the incorporation of amyloid fibrils significantly reduced nanoparticle aggregation and increased the degree of methylene blue conversion, while also lowering the activation energy.
JOURNAL OF THE TAIWAN INSTITUTE OF CHEMICAL ENGINEERS
(2021)
Article
Biochemistry & Molecular Biology
Gabriel Zazeri, Ana Paula Ribeiro Povinelli, Nathalia Mariana Pavan, Alan M. Jones, Valdecir Farias Ximenes
Summary: This study highlights the crucial role of the surrounding environment in influencing amyloid formation. The presence of acetone creates an unfavorable microenvironment for amyloid fibril formation, resulting in the destabilization of the lysozyme protofibril and the inhibition of fibril formation.
Article
Biochemistry & Molecular Biology
Husnul Fuad Zein, Thana Sutthibutpong
Summary: Atomistic molecular dynamics simulations were used to study the effects of charged residues and pH on amyloid models. The simulations revealed that antiparallel configurations had greater stability and compactness compared to parallel configurations. The study also provided insights into the importance of specific residues and the disruption of interaction networks in amyloid formation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Chemistry, Multidisciplinary
Soumav Nath, Priti Roy, Raki Mandal, Rajat Roy, Alexander K. Buell, Neelanjana Sengupta, Pradip K. Tarafdar
Summary: The study demonstrates the potential anti-amyloidogenic properties of endogenously derived compounds based on porphyrin, which can inhibit fibril formation of insulin and hen egg white lysozyme. Hematoporphyrin, derived from heme by hydroxylation and metal removal, shows superior inhibitory effects on insulin fibril formation compared to hemin and protoporphyrin.
CHEMISTRY-AN ASIAN JOURNAL
(2021)
Article
Biochemistry & Molecular Biology
Kanchana Karunarathne, Nabila Bushra, Olivia Williams, Imad Raza, Laura Tirado, Diane Fakhre, Fadia Fakhre, Martin Muschol
Summary: The deposition of dense fibril plaques is a pathological hallmark for various human disorders. Research has focused on understanding the growth of individual fibrils and oligomers, but little is known about the mechanisms of assembly into larger suprastructures. pH and salt play a role in regulating the transition from 3D to 2D fibril self-assembly, which is important for understanding disease pathology and biomaterial applications.
Article
Biochemistry & Molecular Biology
Mohammed J. Hakeem, Javed Masood Khan, Ajamaluddin Malik, Fohad Mabood Husain, Vivek Ambastha
Summary: Several food dyes, including sunset yellow, can induce amyloid fibrillation in proteins such as hen egg white lysozyme (HEWL). This study found that sunset yellow dye induced fast aggregation in HEWL without a lag phase, following an isodesmic pathway. The aggregates had a cross-beta secondary structure and were affected by salts and solvents. The results suggest that electrostatic and hydrophobic interactions play a role in sunset yellow-induced amyloid fibrillation.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Spectroscopy
Natalia Hachlica, Aleksandra Kolodziejczyk, Michal Rawski, Marcin Gorecki, Aleksandra Wajda, Agnieszka Kaczor
Summary: Environmental factors can compete against the templated growth of amyloid fibrils, and the structural indeterminism originates from deeper levels of the fibril structure.
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
(2024)
Article
Biochemistry & Molecular Biology
Daisuke Takahashi, Eri Matsunaga, Tomohiro Yamashita, Jose M. M. Caaveiro, Yoshito Abe, Tadashi Ueda
Summary: In this study, an in-vitro screening system was established to identify inhibitors against AL amyloidosis. Two compounds, gossypetin and isoquercitrin, were found to directly interact with the target protein and enhance its kinetic stability, making them potential leads for developing drugs against AL amyloidosis.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2022)
Article
Biochemistry & Molecular Biology
Maksim I. Sulatsky, Mikhail V. Belousov, Anastasiia O. Kosolapova, Ekaterina V. Mikhailova, Maria N. Romanenko, Kirill S. Antonets, Irina M. Kuznetsova, Konstantin K. Turoverov, Anton A. Nizhnikov, Anna I. Sulatskaya
Summary: Functional amyloids found in plants, particularly vicilin amyloids, have been shown to inhibit the formation of pathological amyloids and decrease their toxicity for mammalian cells, except for insulin.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Chemistry, Multidisciplinary
Natalia Hachlica, Michal Rawski, Marcin Gorecki, Aleksandra Wajda, Agnieszka Kaczor
Summary: In this study, we characterized the organization levels of amyloid fibrils from proteins with similar structures using various methods including VCD, ECD, cryo-EM, and TEM. Our results showed that small changes in protein structure or preparation conditions led to significant differences in the structure and architecture of the fibrils. Although the secondary structure and protofilament twist varied, the mesoscopic structure of the fibrils remained relatively similar. These findings contribute to understanding the indeterministic nature of fibril formation.
CHEMISTRY-A EUROPEAN JOURNAL
(2023)
Article
Biochemistry & Molecular Biology
Joel N. Buxbaum, Angela Dispenzieri, David S. Eisenberg, Marcus Faendrich, Giampaolo Merlini, Maria J. M. Saraiva, Yoshiki Sekijima, Per Westermark
Summary: The Nomenclature Committee of the International Society of Amyloidosis has proposed a nomenclature recommendation, adding six new proteins to the list of human amyloid fibril proteins, including intracellular amyloid fibrils associated with neurodegenerative diseases.
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
(2022)
Article
Biochemistry & Molecular Biology
You-Ren Lai, Jinn-Tsyy Lai, Steven S. -S. Wang, Yung-Chih Kuo, Ta-Hsien Lin
Summary: Protein nanofibers are promising immobilization platforms/substrates for catalysts/enzymes due to their unique structural characteristics and superior biocompatibility. In this study, amyloid fibrils derived from whey protein isolate were used as supports for silver nanoparticles, and the resulting hybrid materials exhibited excellent catalytic performance for the reduction of methylene blue. The characterization and analysis of the materials provided insights into the catalytic mechanism and reusability of the composite materials.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biochemistry & Molecular Biology
Su-Chun How, Ta-Hsien Lin, Chun-Chao Chang, Steven S-S Wang
Summary: In this study, beta-lactoglobulin (β-LG) combined with bovine serum albumin (BSA) was utilized to prepare amyloid-based hydrogels for riboflavin delivery. The presence of BSA enhanced β-LG fibril formation but also interfered with the entanglement of fibril chains, affecting the mechanical properties of the hydrogels. The number of amyloid fibrils was found to positively correlate with the mechanical properties of the hydrogels.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Hsiao-Chieh Tsai, Ching-Hong Huang, Ling-Hsien Tu
Summary: Islet amyloid polypeptide (IAPP) is a polypeptide hormone co-secreted with insulin by pancreatic beta-cells. It tends to aggregate into soluble oligomers, which are considered one of the hallmarks of type II diabetes. This study successfully grafted the aggregation-induced emission molecule TPE onto IAPP, allowing real-time monitoring of IAPP oligomer formation and potential application in the diagnosis of T2D.
BIOPHYSICAL CHEMISTRY
(2024)
Article
Biochemistry & Molecular Biology
Aristeidis Papagiannopoulos, Aggeliki Sklapani, Nikolaos Spiliopoulos
Summary: This study presents a method for preparing Hb-based nanoparticles (NPs) using a fully biocompatible approach. These NPs have a spherical structure with a diameter ranging from 50 to 100 nm, and can form electrostatic complexes with CS at pH 4. The NPs can be pH-tunable and stable in solutions with high salt content, making them suitable for nanodelivery of nutrients and drugs.
BIOPHYSICAL CHEMISTRY
(2024)
Article
Biochemistry & Molecular Biology
Andrey V. Struts, Alexander V. Barmasov, Steven D. E. Fried, Kushani S. K. Hewage, Suchithranga M. D. C. Perera, Michael F. Brown
Summary: This article summarizes and reviews the osmotic stress studies of G-protein-coupled receptor rhodopsin. It is found that water plays an important role in the activation of the receptor, with at least 80 water molecules entering the receptor in the transition to the active state. If water influx is prevented, the functional transition of the receptor is reversed. These findings reveal the phenomenon of solvent swelling in the activation mechanism of rhodopsin, with water acting as an allosteric modulator of function for rhodopsin-like receptors in lipid membranes.
BIOPHYSICAL CHEMISTRY
(2024)
Article
Biochemistry & Molecular Biology
Maria Chiara Saija, Adela Melcrova, Wojciech Pajerski, Itay Schachter, Matti Javanainen, Marek Cebecauer, Lukasz Cwiklik
Summary: We used molecular dynamics simulations to investigate the effects of palmitoylation on a transmembrane peptide in different lipid environments. The study found that palmitoylation reduces the peptide's impact on membrane thickness, particularly in lipid-ordered and boundary environments. The hydrophobic palmitoyl chains on the peptide did not significantly affect membrane hydration. Interestingly, the boundary membrane environment was found to be highly compatible with the palmitoylated peptide. These findings have important implications for understanding cell signaling, membrane organization, and optimizing lipid membrane-based drug delivery systems.
BIOPHYSICAL CHEMISTRY
(2024)
Article
Biochemistry & Molecular Biology
Achanta Rishisree, Brayer Mallory, Karnaukhova Elena, Jankovic Teodora, Zdunic Gordana, Savikin Katarina, Jeremic Aleksandar
Summary: Pomegranate peel, ironwort, and chokeberry leaf extracts exhibit anti-aggregative and antitoxic properties against human amylin. They can prevent amyloidosis and cell loss in patients with Type 2 Diabetes Mellitus.
BIOPHYSICAL CHEMISTRY
(2024)
