Publicaciones 2011-2020

@article{RN387,
title = {Telomerase Inhibition by a New Synthetic Derivative of the Aporphine Alkaloid Boldine},
author = { S.K. Noureini and M. Kheirabadi and F. Masoumi and F. Khosrogerdi and Y. Zarei and C. Suarez-Rozas and J. Salas-Norambuena and B.K. Cassels},
url = {/brokenurl#<Go to ISI>://WOS:000434978700318},
doi = {10.3390/ijms19041239},
issn = {1422-0067},
year = {2018},
date = {2018-01-01},
journal = {International Journal of Molecular Sciences},
volume = {19},
number = {4},
abstract = {Telomerase, the enzyme responsible for cell immortality, is an important target in anti-cancer drug discovery. Boldine, an abundant aporphine alkaloid of Peumus boldus, is known to inhibit telomerase at non-toxic concentrations. Cytotoxicity of N-benzylsecoboldine hydrochloride (BSB), a synthetic derivative of boldine, was determined using the MTT method in MCF7 and MDA-MB231 cells. Aliquots of cell lysates were incubated with various concentrations of BSB in qTRAP (quantitative telomere repeat amplification protocol)-ligand experiments before substrate elongation by telomerase or amplification by hot-start Taq polymerase. The crystal structure of TERT, the catalytic subunit of telomerase from Tribolium castaneum, was used for docking and molecular dynamics analysis. The qTRAP-ligand data gave an IC50 value of about 0.17 +/- 0.1 mu M for BSB, roughly 400 times stronger than boldine, while the LD50 in the cytotoxicity assays were 12.5 and 21.88 mu M, respectively, in cells treated for 48 h. Although both compounds interacted well with the active site, MD analysis suggests a second binding site with which BSB interacts via two hydrogen bonds, much more strongly than boldine. Theoretical analyses also evaluated the IC50 for BSB as submicromolar. BSB, with greater hydrophobicity and flexibility than boldine, represents a promising structure to inhibit telomerase at non-toxic concentrations.},
keywords = {apoptosis, assay binding boldine, cells, derivative, domain, inhibition, n-benzylsecoboldine, site, stress, telomerase},
pubstate = {published},
tppubtype = {article}
}

@article{RN193,
title = {A Coumarinylaldoxime as a Specific Sensor for Cu2+ and Its Biological Application},
author = { O. Garcia-Beltran and B.K. Cassels and N. Mena and M. Nunez and O. Yanez and J. Caballero},
url = {/brokenurl#<Go to ISI>://WOS:000330604500023},
doi = {10.1016/j.tetlet.2013.12.033},
issn = {0040-4039},
year = {2014},
date = {2014-01-01},
journal = {Tetrahedron Letters},
volume = {55},
number = {4},
pages = {873-876},
publisher = {2013 Elsevier Ltd.},
abstract = {In this Letter we present a new probe, (E)-7-(diethylamino)-2-oxo-2H-chromene-3-carbaldehyde oxime (JB), which can detect Cu2+ ions in HEPES buffer under physiological conditions. Benesi-Hildebrand and Job plots demonstrate that the stoichiometry of the Cu2+ complex formed is 2:1. Possible interference with other analytes was examined, and the decrease of the fluorescence of JB at 510 nm when it reacts with Cu2+ was shown to be highly selective. This probe accumulates in the plasmalemma of human neuroblastoma SH-SY5Y cells. Molecular dynamics (MD) simulations revealed thatJB interacts with the lipid bilayer at the level of the glycerol moieties.},
keywords = {bilayer, copper, coumarin cu2+-selectivity, derivative, design, dynamics, fluorescent lipid membranes molecular probe},
pubstate = {published},
tppubtype = {article}
}