Zhou et al., 2023 - Google Patents
Sodium oligomannate electrostatically binds to Aβ and blocks its aggregationZhou et al., 2023
- Document ID
- 3618200035607825019
- Author
- Zhou C
- Zhang J
- Luo X
- Lian F
- Zeng Y
- Zhang Z
- Zhang H
- Zhang N
- Publication year
- Publication venue
- The Journal of Physical Chemistry B
External Links
Snippet
GV-971 (sodium oligomannate) is a China Food and Drug Administration (CFDA)-approved drug for treating Alzheimer's disease, and it could inhibit Aβ fibril formation in vitro and in mouse studies. To elucidate the mechanisms for understanding how GV-971 modulates Aβ's …
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4711—Alzheimer's disease; Amyloid plaque core protein
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2828—Prion diseases
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2821—Alzheimer
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Willbold et al. | Amyloid-type protein aggregation and prion-like properties of amyloids | |
Hubin et al. | Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease | |
Okada et al. | Toxic amyloid tape: a novel mixed antiparallel/parallel β-sheet structure formed by amyloid β-protein on GM1 clusters | |
Broersen et al. | The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? | |
Salomon et al. | Nicotine inhibits amyloid formation by the β-peptide | |
Sinha et al. | A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity | |
Karr et al. | Cu (II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer’s disease amyloid-β peptide | |
Zhang et al. | Molecular understanding of Aβ-hIAPP cross-seeding assemblies on lipid membranes | |
Vosough et al. | Characterization of homogeneous and heterogeneous amyloid-β42 oligomer preparations with biochemical methods and infrared spectroscopy reveals a correlation between infrared spectrum and oligomer size | |
Das et al. | Looking at the disordered proteins through the computational microscope | |
Mannini et al. | Stabilization and characterization of cytotoxic Aβ40 oligomers isolated from an aggregation reaction in the presence of zinc ions | |
Yamaguchi et al. | A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation | |
Xu et al. | Curcumin interacts with α-synuclein condensates to inhibit amyloid aggregation under phase separation | |
Dou et al. | Phosphatidylcholine and phosphatidylserine uniquely modify the secondary structure of α-synuclein oligomers formed in their presence at the early stages of protein aggregation | |
Hou et al. | Inhibition of β-amyloid channels with a drug candidate wgx-50 revealed by molecular dynamics simulations | |
Abelein et al. | Molecular structure of Cu (II)-bound amyloid-β monomer implicated in inhibition of peptide self-assembly in Alzheimer’s disease | |
Foley et al. | Trapping and characterization of nontoxic Aβ42 aggregation intermediates | |
de Almeida et al. | Opposing effects of cucurbit [7] uril and 1, 2, 3, 4, 6-penta-O-galloyl-β-d-glucopyranose on amyloid β25–35 assembly | |
Mohamed et al. | Tau derived hexapeptide AcPHF6 promotes beta-amyloid (Aβ) fibrillogenesis | |
Pham et al. | Copper binding induces polymorphism in amyloid-β peptide: Results of computational models | |
Baram et al. | Inhibitory activity of insulin on Aβ aggregation is restricted due to binding selectivity and specificity to polymorphic Aβ states | |
Korn et al. | Incorporation of the nonproteinogenic amino acid β-methylamino-alanine affects amyloid β fibril properties and toxicity | |
Banerjee et al. | Nanoscale infrared spectroscopy identifies structural heterogeneity in individual amyloid fibrils and prefibrillar aggregates | |
Williams et al. | Soluble prion protein binds isolated low molecular weight amyloid-β oligomers causing cytotoxicity inhibition | |
Zhou et al. | Sodium oligomannate electrostatically binds to Aβ and blocks its aggregation |