Publicaciones 2011-2020

@article{RN337,
title = {Rosmarinic Acid Prevents Fibrillization and Diminishes Vibrational Modes Associated to Beta Sheet in Tau Protein Linked to Alzheimer's Disease},
author = { A. Cornejo and F.A. Sandoval and L. Caballero and L. Machuca and P. Munoz and J. Caballero and G. Perry and A. Ardiles and C. Areche and F. Melo},
url = {/brokenurl#<Go to ISI>://WOS:000406130000006},
doi = {10.1080/14756366.2017.1347783},
issn = {1475-6366},
year = {2017},
date = {2017-01-01},
journal = {Journal of Enzyme Inhibition and Medicinal Chemistry},
volume = {32},
number = {1},
pages = {945-953},
abstract = {Alzheimer's disease is a common tauopathy where fibril formation and aggregates are the hallmark of the disease. Efforts targeting amyloid-beta plaques have succeeded to remove plaques but failed in clinical trials to improve cognition; thus, the current therapeutic strategy is at preventing tau aggregation. Here, we demonstrated that four phenolic diterpenoids and rosmarinic acid inhibit fibrillization. Since, rosmarinic acid was the most active compound, we observe morphological changes in atomic force microscopy images after treatment. Hence, rosmarinic acid leads to a decrease in amide regions I and III, indicating that rosmarinic acid prevents beta-sheet assembly. Molecular docking study inside the steric zipper model of the hexapeptide (306)VQIVYK(311) involved in fibrillization and beta sheet formation, suggests that rosmarinic acid binds to the steric zipper with similar chemical interactions with respect to those observed for orange G, a known pharmacofore for amyloid.},
keywords = {alzheimer's amyloid beta-sheet, carnosic cells criteria, disease, fibril filaments, formation, helical in-vitro, inhibition, inhibitors, mice, neuropathologic paired pharmacophore, salvia-officinalis, tau transgenic},
pubstate = {published},
tppubtype = {article}
}

@article{RN286,
title = {Secondary Metabolites in Ramalina Terebrata Detected by Uhplc/Esi/Ms/Ms and Identification of Parietin as Tau Protein Inhibitor},
author = { A. Cornejo and F. Salgado and J. Caballero and R. Vargas and M. Simirgiotis and C. Areche},
url = {/brokenurl#<Go to ISI>://WOS:000382337900115},
doi = {10.3390/ijms17081303},
issn = {1422-0067},
year = {2016},
date = {2016-01-01},
journal = {International Journal of Molecular Sciences},
volume = {17},
number = {8},
abstract = {Liquid chromatography coupled with mass spectrometry is an outstanding methodology for fast analysis of phenolic compounds in biological samples. Twenty two compounds were quickly and accurately identified in the methanolic extract of the Antarctic lichen Ramalina terebrata for the first time using ultra high pressure liquid chromatography coupled with photodiode array detector and high resolution mass spectrometry (UHPLC-PDA-Q/Orbitrap/MS/MS). In addition, the extract and the four compounds isolated from this species were tested for the inhibitory activity of tau protein aggregation, which is a protein involved in Alzheimer's disease (AD). All compounds showed null activity with the exception of parietin, which it was able to inhibit aggregation process of tau in a concentration range between 3 mu g/mL (10 mu M) to 28 mu g/mL (100 mu M). In addition, we show how parietin interact with tau (306)VQIVYK(311) hexapeptide inside of the microtubule binding domain (4R) with the help of molecular docking experiments. Finally, the constituents present in the methanolic extract could possibly contribute to the established anti-aggregation activity for this extract and this in-depth analysis of the chemical composition of R. terebrata could guide further research into its medicinal properties and potential uses.},
keywords = {alzheimer's alzheimers-disease, biological disease, docking, evaluation, fibril filaments, formation helical lichen lichens, liquid-chromatography, mass-spectrometry, molecular paired parietin, phenolic-compounds, protein, ramalina, tau uhplc-q/orbitrap/ms/ms, uhplc/ms, xanthoria-parietina},
pubstate = {published},
tppubtype = {article}
}