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  1. Home
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Browsing by Author "Garrido, J."

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    Access to New Cytotoxic Quinone-Amino Acid Conjugates Linked through A Vinylic Spacer from 2-Acylnaphthoquinones and Methyl 3-Aminocrotonate
    (2017) Valderrama, J.; Garrido, J.; Delgado Chang, Virginia; Benites, J.; Theoduloz, C.
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    Hyperforin prevents β-amyloid neurotoxicity and spatial memory impairments by disaggregation of Alzheimer's amyloid-β-deposits
    (2006) Dinamarca, M. C.; Cerpa, W.; Garrido, J.; Hancke, J. L.; Inestrosa, N. C.
    The major protein constituent of amyloid deposits in Alzheimer's disease (AD) is the amyloid beta-peptide (A beta). In the present work, we have determined the effect of hyperforin an acylphloroglucinol compound isolated from Hypericum perforatum (St John's Wort), on A beta-induced spatial memory impairments and on A beta neurotoxicity. We report here that hyperforin: ( 1) decreases amyloid deposit formation in rats injected with amyloid fibrils in the hippocampus; ( 2) decreases the neuropathological changes and behavioral impairments in a rat model of amyloidosis; ( 3) prevents A beta-induced neurotoxicity in hippocampal neurons both from amyloid fibrils and A beta oligomers, avoiding the increase in reactive oxidative species associated with amyloid toxicity. Both effects could be explained by the capacity of hyperforin to disaggregate amyloid deposits in a dose and time-dependent manner and to decrease A beta aggregation and amyloid formation. Altogether these evidences suggest that hyperforin may be useful to decrease amyloid burden and toxicity in AD patients, and may be a putative therapeutic agent to fight the disease.

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