Results 1 to 10 of about 28,974 (147)
Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations. [PDF]
PLoS ONE, 2016 We report here interesting synergistic effects of proline and sorbitol, two well-known chemical chaperones, in the inhibition of fibrillation of two proteins, insulin and lysozyme.
Sinjan Choudhary +3 more
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Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq
Antibiotics, 2021 Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance
Florian Turbant +6 more
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Protein Fibrillation Lag Times During Kinetic Inhibition [PDF]
Biophysical Journal, 2014 Protein aggregation is linked to more than 30 human pathologies, including Alzheimer's and Parkinson's diseases. Since small oligomers that form at the beginning of the fibrillation process probably are the most toxic elements, therapeutic strategies involving fibril fragmentation could be detrimental. An alternative approach, named kinetic inhibition,
Pagano, Rodrigo Sebastián +7 more
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Journal of Disability Research, 2023 The study aims to examine the aggregation of proteins due to their association with various conformational problems including well-known neurodegenerative diseases like Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease.
Nada H. Aljarba +3 more
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Inhibiting transthyretin amyloid fibril formation via protein stabilization [PDF]
Proceedings of the National Academy of Sciences, 1996 Transthyretin (TTR) amyloid fibril formation is observed systemically in familial amyloid polyneuropathy and senile systemic amyloidosis and appears to be the causative agent in these diseases. Herein, we demonstrate conclusively that thyroxine (10.8 μM) inhibits TTR fibril formation efficiently in vitro and ...
G J, Miroy +5 more
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Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins [PDF]
Prion, 2010 Several neurodegenerative diseases involve the selective damage of neuron cells resulting from the accumulation of amyloid fibril formation. Considering that the formation of amyloid fibrils as well as their precursor oligomers is cytotoxic, the agents that prevent the formation of oligomers and/or fibrils might allow the development of a novel ...
Jihoon, Kim +10 more
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Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition
Molecules, 2022 Most neurodegenerative diseases such as Alzheimer’s disease, type 2 diabetes, Parkinson’s disease, etc. are caused by inclusions and plaques containing misfolded protein aggregates.
Sushma Subedi +4 more
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Aggregation of an Amyloidogenic Peptide on Gold Surfaces
Biomolecules, 2023 Solid surfaces have been shown to affect the aggregation and assembly of many biomolecular systems. One important example is the formation of protein fibrils, which can occur on a range of biological and synthetic surfaces.
David L. Cheung
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Selective inhibition of aggregation/fibrillation of bovine serum albumin by osmolytes: Mechanistic and energetics insights. [PDF]
PLoS ONE, 2017 Bovine serum albumin (BSA) is an important transport protein of the blood and its aggregation/fibrillation would adversely affect its transport ability leading to metabolic disorder.
Moumita Dasgupta, Nand Kishore
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iScience, 2020 Summary: Amyloid are protein aggregates formed by cross β structures assemblies. Inhibiting amyloid aggregation or facilitating its disassembly are considered to be two major effective therapeutic strategies in diseases involving peptide or protein ...
Siqi Wang +9 more
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