McCarthy et al., 2013 - Google Patents
Influence of surface groups on poly (propylene imine) dendrimers antiprion activityMcCarthy et al., 2013
View PDF- Document ID
- 258871287484316724
- Author
- McCarthy J
- Rasines Moreno B
- Filippini D
- Komber H
- Maly M
- Cernescu M
- Brutschy B
- Appelhans D
- Rogers M
- Publication year
- Publication venue
- Biomacromolecules
External Links
Snippet
Prion diseases are characterized by the accumulation of PrPSc, an aberrantly folded isoform of the host protein PrPC. Specific forms of synthetic molecules known as dendrimers are able to eliminate protease-resistant PrPSc in both an intracellular and in vitro setting. The …
- 229920000333 poly(propyleneimine) 0 title abstract description 72
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
-
- 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
- G01N33/5008—Chemical 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
- G01N33/502—Chemical 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
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay
- G01N33/543—Immunoassay; Biospecific binding assay with an insoluble carrier for immobilising immunochemicals
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
- A61K47/48—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/48—Preparations in capsules, e.g. of gelatin, of chocolate
- A61K9/50—Microcapsules having a gas, liquid or semi-solid filling; Solid microparticles or pellets surrounded by a distinct coating layer, e.g. coated microspheres, coated drug crystals
- A61K9/51—Nanocapsules; Nanoparticles
- A61K9/5107—Excipients; Inactive ingredients
- A61K9/513—Organic macromolecular compounds; Dendrimers
- A61K9/5146—Organic macromolecular compounds; Dendrimers obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyethylene glycol, polyamines, polyanhydrides
- A61K9/5153—Polyesters, e.g. poly(lactide-co-glycolide)
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| McCarthy et al. | Influence of surface groups on poly (propylene imine) dendrimers antiprion activity | |
| Lin et al. | Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions | |
| Fischer et al. | Influence of surface functionality of poly (propylene imine) dendrimers on protease resistance and propagation of the scrapie prion protein | |
| Narayan et al. | Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells | |
| Mosquera et al. | Reversible control of protein corona formation on gold nanoparticles using host–guest interactions | |
| Grassmann et al. | Cellular aspects of prion replication in vitro | |
| Siddiqua et al. | Conformational basis for asymmetric seeding barrier in filaments of three-and four-repeat tau | |
| Shi et al. | Effect of polyplex morphology on cellular uptake, intracellular trafficking, and transgene expression | |
| Kelly et al. | Poly (amidoamine) dendrimers on lipid bilayers II: Effects of bilayer phase and dendrimer termination | |
| Wang et al. | Understanding effects of PAMAM dendrimer size and surface chemistry on serum protein binding with discrete molecular dynamics simulations | |
| Zhang et al. | Interaction of polyethylenimine with model cell membranes studied by linear and nonlinear spectroscopic techniques | |
| Assarsson et al. | Effects of polyamino acids and polyelectrolytes on amyloid β fibril formation | |
| Kakish et al. | Drugs that bind to α-synuclein: neuroprotective or neurotoxic? | |
| Hirano et al. | Adsorption and disruption of lipid bilayers by nanoscale protein aggregates | |
| Dai et al. | Cell-conditioned protein coronas on engineered particles influence immune responses | |
| Heo et al. | ATP kinetically modulates pathogenic tau fibrillations | |
| Kaur et al. | Membrane interactions of α-synuclein probed by neutrons and photons | |
| Pan et al. | Lipid extraction by α-synuclein generates semi-transmembrane defects and lipoprotein nanoparticles | |
| Wang et al. | Mixed carboxyl and hydrophobic dendrimer surface inhibits amyloid-β fibrillation: New insight from the generation number effect | |
| Sorokina et al. | Dendrimers as antiamyloid agents | |
| Cifuentes et al. | Multifunctional magnetoliposomes as drug delivery vehicles for the potential treatment of Parkinson’s disease | |
| Mohammad-Beigi et al. | A protein corona modulates interactions of α-synuclein with nanoparticles and alters the rates of the microscopic steps of amyloid formation | |
| Williams et al. | Soluble prion protein binds isolated low molecular weight amyloid-β oligomers causing cytotoxicity inhibition | |
| Ojha et al. | Poly (4-styrenesulfonate) as an inhibitor of Aβ40 amyloid fibril formation | |
| Prior et al. | Cyclodextrins inhibit replication of scrapie prion protein in cell culture |