Journal of Medicinal Chemistry · 2006 · 12 citations · 11 references
PharmacyBiochemistryMedicinal ChemistryDrug DesignDrug DiscoveryNeurodegenerationAlzheimer DiseaseAmyloid FormationNeurodegenerative Disease PharmacotherapyPeptide ChemistryPeptide Drug DiscoveryPeptide ProdrugsAmyloid Beta AggregationAmyloid Beta PeptidesAmyloid Fibril FormationAmyloid FibrilsAmyloid StructureAmyloid-associated NeurotoxicityAmyloid-beta-induced NeurotoxicityInhibition Of Amyloid Formation
A peptide chAbeta30-16 (15-mer; CTFVRTHIFCKEHQF) was designed to bind to a region encompassing the entire polymerization-related (16KLVFF20) and part of the polymerization and toxicity-related (25GSNKGAIIGLM35) regions of amyloid beta-protein, Abeta1-42 by a hydropathic complementary approach. This peptide efficiently binds to Abeta and blocks intermolecular interaction and the formation of Abeta aggregates. In addition, the peptide neutralizes the cell toxicity of Abeta fibrils. The chAbeta30-16 peptide or its derivatives may be a starting point for the future development of drugs that prevent the neurotoxicity and deposition of Abeta in the brain of Alzheimer's disease.
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John J. Balbach, Yoshitaka Ishii, Oleg N. Antzutkin et al. · Biochemistry · 2000 · 703 citations
A Strategy for Designing Inhibitors of β-Amyloid Toxicity
Jyothi Ghanta, Chih-Lung Shen, Laura L. Kiessling et al. · Journal of Biological Chemistry · 1996 · 223 citations · Full text
Complementary hydropathy identifies a cellular prion protein receptor
Vilma R. Martins, Edgard Graner, José Garcia-Abreu et al. · Nature Medicine · 1997 · 184 citations