Thiosemicarbazonate complexes with affinity for amyloid-β fibers: synthesis, characterization and biological studies
| Autor: | Ezequiel M. Vázquez-López, Arantxa Pino-Cuevas, António Paulo, Paula D. Raposinho, Rosa Carballo, Ulrich Abram, Célia Fernandes |
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| Rok vydání: | 2019 |
| Předmět: |
Thiosemicarbazones
Pharmacology Amyloid beta-Peptides Biological studies Molecular Structure Amyloid Amyloid β 010405 organic chemistry Chemistry Stereochemistry Brain chemistry.chemical_element Rhenium Ligands 010402 general chemistry 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Azobenzene Drug Discovery Humans Molecular Medicine Radiopharmaceuticals Semicarbazone |
| Zdroj: | Future Medicinal Chemistry. 11:2527-2546 |
| ISSN: | 1756-8927 1756-8919 |
| DOI: | 10.4155/fmc-2019-0013 |
| Popis: | Aim: Obtain radioimages of amyloid-β fibers using 99mTc-complexes. Methodology: Tridentate thiosemicarbazone and thiocarbonohydrazone ligands containing fragments (stilbene, azobenzene, benzothiazole or benzoxazole) with affinity for amyloid-ß fibers and its Re(I) complexes have been prepared. The molecular structures of several ligands and complexes were determined by x-ray diffraction. Binding affinity studies toward Aß1-42 fibers were performed for the ligands and Re(I) complexes. The ability of formation of some 99mTc(I) complexes, their biodistribution and in vivo stability have been established. Results & conclusion: Complexes of stilbene and benzothiazole thiosemicarbazonates show similar affinity for amyloid-β fibers to the free ligand. These 99mTc complexes present a reasonable in vivo stability and a low capability to cross the blood–brain barrier although not sufficient to brain amyloid imaging. |
| Databáze: | OpenAIRE |
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