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Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid

BAURES, P. W ; OZA, V. B ; PETERSON, S. A ; KELLY, J. W

Bioorganic & medicinal chemistry, 1999-07, Vol.7 (7), p.1339-1347 [Periódico revisado por pares]

Oxford: Elsevier Science

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Título:
Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
Autor: BAURES, P. W ; OZA, V. B ; PETERSON, S. A ; KELLY, J. W
Assuntos: Amyloid - drug effects ; Amyloid - metabolism ; Amyloid - ultrastructure ; Amyloidosis ; Anti-Inflammatory Agents, Non-Steroidal - chemical synthesis ; Anti-Inflammatory Agents, Non-Steroidal - metabolism ; Anti-Inflammatory Agents, Non-Steroidal - pharmacology ; Binding Sites ; Biological and medical sciences ; Diflunisal - chemistry ; Diflunisal - pharmacology ; Drug Design ; Drug Evaluation, Preclinical ; Flufenamic Acid - chemistry ; Flufenamic Acid - metabolism ; Flufenamic Acid - pharmacology ; Humans ; Light ; Medical sciences ; Metabolic diseases ; Miscellaneous ; Neuropharmacology ; Niflumic Acid - chemistry ; Niflumic Acid - pharmacology ; Other metabolic disorders ; Pharmacology. Drug treatments ; Prealbumin - antagonists & inhibitors ; Prealbumin - chemistry ; Prealbumin - metabolism ; Scattering, Radiation ; Structure-Activity Relationship ; Sulindac - chemistry ; Sulindac - pharmacology ; Tolmetin - chemistry ; Tolmetin - pharmacology
É parte de: Bioorganic & medicinal chemistry, 1999-07, Vol.7 (7), p.1339-1347
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: A light scattering-based amyloid fibril formation assay was employed to evaluate potential inhibitors of transthyretin (TTR) amyloid fibril formation in vitro. Twenty nine aromatic small molecules, some with homology to flufenamic acid (a known non-steroidal anti-inflammatory drug) were tested to identify important structural features for inhibitor efficacy. The results of these experiments and earlier data suggest that likely inhibitors will have aromatic-based structures with at least two aromatic rings. The ring or fused ring system occupying the outermost TTR binding pocket needs to be substituted with an acidic functional group (e.g. a carboxylic acid) to interact with complimentary charges in the TTR binding site. The promising TTR amyloid fibril inhibitors ranked in order of efficacy are: 2 > 4 approximately 7 > 3 > 9 > 6 > 21.
Editor: Oxford: Elsevier Science
Idioma: Inglês

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Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid

BAURES, P. W ; OZA, V. B ; PETERSON, S. A ; KELLY, J. W

Oxford: Elsevier Science

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