[go: up one dir, main page]

Gorantla et al., 2019 - Google Patents

Molecular cobalt (II) complexes for tau polymerization in Alzheimer's disease

Gorantla et al., 2019

View PDF @Full View
Document ID
4960262903242711217
Author
Gorantla N
Landge V
Nagaraju P
Priyadarshini CG P
Balaraman E
Chinnathambi S
Publication year
Publication venue
ACS omega

External Links

Snippet

Tau is an axonal protein known to form abnormal aggregates and is the biomarker of Alzheimer's disease. Metal-based therapeutics for inhibition of Tau aggregation is limited and rarely reported in contemporary science. Here, we report the first example of rationally …
Continue reading at pubs.acs.org (PDF) (other versions)

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • G01N33/5008Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
    • G01N33/502Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6893Chemical 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
    • G01N33/6896Neurological disorders, e.g. Alzheimer's disease
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00Medicinal preparations containing organic active ingredients
    • A61K31/33Heterocyclic compounds
    • A61K31/395Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine, rifamycins
    • A61K31/41Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine, rifamycins having five-membered rings with two or more ring hetero atoms, at least one of which being nitrogen, e.g. tetrazole
    • A61K31/425Thiazoles
    • A61K31/428Thiazoles condensed with carbocyclic rings
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00Medicinal preparations containing organic active ingredients
    • A61K31/33Heterocyclic compounds
    • A61K31/335Heterocyclic compounds having oxygen as the only ring hetero atom, e.g. fungichromin
    • A61K31/336Heterocyclic compounds having oxygen as the only ring hetero atom, e.g. fungichromin having three-membered rings, e.g. oxirane, fumagillin
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00Medicinal preparations containing organic active ingredients
    • A61K31/185Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic, hydroximic acids
    • A61K31/19Carboxylic acids, e.g. valproic acid

Similar Documents

Publication Publication Date Title
Gorantla et al. Molecular cobalt (II) complexes for tau polymerization in Alzheimer’s disease
Han et al. Mechanistic insight into the design of chemical tools to control multiple pathogenic features in Alzheimer’s disease
Pagano et al. Natural compounds as inhibitors of Aβ peptide aggregation: chemical requirements and molecular mechanisms
Kim et al. EPPS rescues hippocampus-dependent cognitive deficits in APP/PS1 mice by disaggregation of amyloid-β oligomers and plaques
Masuda et al. Small molecule inhibitors of α-synuclein filament assembly
Verwilst et al. Rational design of in vivo tau tangle-selective near-infrared fluorophores: expanding the BODIPY universe
Batkulwar et al. Advanced glycation end products modulate amyloidogenic APP processing and tau phosphorylation: a mechanistic link between glycation and the development of Alzheimer’s disease
Bolognesi et al. ANS binding reveals common features of cytotoxic amyloid species
Sinha et al. Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins
Du et al. Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity
Wu et al. Sequestration of copper from β-amyloid promotes selective lysis by cyclen-hybrid cleavage agents
Bitan et al. Rapid photochemical cross-linking a new tool for studies of metastable, amyloidogenic protein assemblies
Faller et al. Role of metal ions in the self-assembly of the Alzheimer’s amyloid-β peptide
Mandal et al. Oxidative stress: glutathione and its potential to protect methionine-35 of Aβ peptide from oxidation
Guan et al. Stereochemistry and amyloid inhibition: asymmetric triplex metallohelices enantioselectively bind to Aβ peptide
Paul et al. Novel mannitol-based small molecules for inhibiting aggregation of α-synuclein amyloids in Parkinson's disease
Kumar et al. α-helix mimetics as modulators of Aβ self-assembly
Sun et al. Amentoflavone: a bifunctional metal chelator that controls the formation of neurotoxic soluble Aβ42 oligomers
Valiente-Gabioud et al. Phthalocyanines as molecular scaffolds to block disease-associated protein aggregation
Ramesh et al. Rationally designed molecules synergistically modulate multifaceted Aβ toxicity, microglial activation, and neuroinflammation
Zhang et al. Study of a bifunctional Aβ aggregation inhibitor with the abilities of antiamyloid-β and copper chelation
Ferrari et al. Synthesis, structure characterization, and evaluation in microglia cultures of neuromelanin analogues suitable for modeling Parkinson’s disease
Vuong et al. Binding of glyco-acridine derivatives to lysozyme leads to inhibition of amyloid fibrillization
Ma et al. Modulating conformation of Aβ-peptide: an effective way to prevent protein-misfolding disease
Wang et al. Thermodynamic analysis of the molecular interactions between amyloid β-protein fragments and (−)-epigallocatechin-3-gallate