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{RN196,
title = {Molecular Characterization and in Silico Analysis of the Pheromone-Binding Protein of the European Grapevine Moth Lobesia Botrana (Denis & Schiffermuller) (Lepidoptera, Tortricidae)},
author = { A. Mutis and R. Palma and H. Venthur and P. Iturriaga-Vasquez and M. Faundez-Parraguez and R. Mella-Herrera and D. Kontodimas and C. Lobos and A. Quiroz},
url = {/brokenurl#<Go to ISI>://WOS:000335640500010},
doi = {10.1007/s13744-014-0212-2},
issn = {1519-566x},
year = {2014},
date = {2014-01-01},
journal = {Neotropical Entomology},
volume = {43},
number = {3},
pages = {266-275},
abstract = {The European grapevine moth Lobesia botrana (Denis & Schiffermuller) is an economically important insect in Europe. The species invaded vineyards in Chile, Argentina, and California during 2008-2010 causing severe problems. A major component of the sex pheromone, (E,Z)-7,9-dodecadienyl acetate (E7,Z9-12:Ac), is used in a mating disruption technique when grapevine moth populations are low or to monitor pest numbers. It is thought that these sexual pheromones are blends of volatiles that typically are specific to a species and are transported in the insect antenna by pheromone-binding proteins (PBPs) across the sensillar lymph to the olfactory receptors. Currently, an increasing number of Lepidopteran PBPs are being identified and cloned. However, there are no studies of the olfactory system and of proteins involved in the olfactory perception of L. botrana at the molecular level. In the present study, we report, for the first time, the sequence of a PBP from L. botrana (LbotPBP), which was determined using reverse transcription technology. Homology modeling was used to generate the three-dimensional protein structure. The model suggests that PBP consists of six alpha-helices as follows: Lys2-Met23 (alpha 1), Thr28-Phe36 (alpha 2), Arg46-Leu59 (alpha 3), His70-Asn80 (alpha 4), Glu84-Asn100 (alpha 5), and Cys108-Lys125 (alpha 6), held together by three disulfide bridges, Cys19-Cys54, Cys50-Cys108, and Cys97-Cys117. Docking simulations based on this model suggested that Trp114 is a keywords residue in the recognition of acetate pheromones, such as E7,Z9-12:Ac. In silico results in this study are consistent with previous findings in which E7,Z9-12:Ac acts as the most active compound in behavioral and electroantennographic assays.},
keywords = {alignment, anopheles-gambiae, antheraea-polyphemus, binding bombyx-mori, chemical crystal-structure, docking, ecology, ligand lymantria-dispar, modeling, molecular multiple nmr pheromone-binding protein, release, sequence sex-pheromone, site, structure, z)-7},
pubstate = {published},
tppubtype = {article}
}

@article{RN169,
title = {Quantum Chemical Study of the Relationships between Electronic Structure and Pharmacokinetic Profile, Inhibitory Strength toward Hepatitis C Virus Ns5b Polymerase and Hcv Replicons of Indole-Based Compounds},
author = { A.P. De La Vega and D.A. Alarcon and J.S. Gomez-Jeria},
url = {/brokenurl#<Go to ISI>://WOS:000331238800051},
doi = {10.4067/S0717-97072013000400055},
issn = {0717-9707},
year = {2013},
date = {2013-01-01},
journal = {Journal of the Chilean Chemical Society},
volume = {58},
number = {4},
pages = {2148-2157},
abstract = {This paper uses newly developed and extended quantum chemical methods in an attempt to advance the knowledge of the relationship between the variation of several local atomic descriptors of the electronic structure and the variation of the inhibitory capacity of a group of reversible and irreversible inhibitors of hepatitis C virus NS5B polymerase. Good structure-activity relationships were obtained for both kinds of compounds. Some processes are charge-, orbital- and/or steric-controlled. The action mechanisms seem to be different for reversible and irreversible inhibitors. Also, good QSAR equations were obtained for the activities of these compounds in a cellular replicon assay and for pharmacokinetic profiles. The local atomic hardness seems to give a good account of the interaction of the drugs with apolar sites of the partner (enzyme, receptor, etc.). This is the first time that a purely quantum-chemical index is able to deal directly with this kind of interaction.},
keywords = {antigenic binding, c chemistry, core crystal-structure, dependent derivatives, discovery, hcv hepatitis ns5b nucleoside nucleotide, pharmacology, polymerase, protein, qsar, quantum replicons, rna-polymerase, site, structure-affinity, virus},
pubstate = {published},
tppubtype = {article}
}