Examinando por Autor "Aguilar-Pineda, J."

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    Identification and Characterization of Peruvian Native Bacterial Strains as Bioremediation of Hg-Polluted Water and Soils Due to Artisanal and Small-Scale Gold Mining in the Secocha Annex, Arequipa
    (MDPI, 2022-02) Fernandez-F, F.; Lopez-C, P.; Febres-Molina, C.; Gamero-Begazo, P.; Gómez, B.; Bernabe-Ortiz, J.; Cáceres-Huambo, A.; Aguilar-Pineda, J.
    The water and soils pollution due to mercury emissions from mining industries represents a serious environmental problem and continuous risk to human health. Although many strategies have been designed for the recovery or elimination of this metal from environmental sources, microbial bioremediation has proven to be the most effective and environmentally friendly strategy and thus control heavy metal contamination. The main objective of this work, using native bacterial strains obtained from contaminated soils of the Peruvian region of Secocha, was to identify which of these strains would have growth capacity on mercury substrates to evaluate their adsorption behavior and mercury removal capacity. Through a DNA analysis (99.78% similarity) and atomic absorption spectrometry, the Gram-positive bacterium Zhihengliuella alba sp. T2.2 was identified as the strain with the highest mercury removal capacity from culture solutions with an initial mercury concentration of 162 mg·L−1 . The removal capacity reached values close to 39.5% in a period of incubation time of 45 days, with maximum elimination efficiency in the first 48 h. These results are encouraging and show that this native strain may be the key to the bioremediation of water and soils contaminated with mercury.
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    Ítem
    In Silico Analysis of the Antagonist Effect of Enoxaparin on the ApoE4–Amyloid-Beta (Aβ) Complex at Different pH Conditions
    (MDPI, 2022-03) Aguilar-Pineda, J.; Paco-Coralla, S.; Febres-Molina, C.; Gamero-Begazo, P.; Shrivastava, P.; Vera-López, K.; Davila-Del-carpio, G.; López-C, P.; Gómez, B.; Lino Cardenas, C.
    Apolipoprotein E4 (ApoE4) is thought to increase the risk of developing Alzheimer’s disease. Several studies have shown that ApoE4-Amyloid β (Aβ) interactions can increment amyloid depositions in the brain and that this can be augmented at low pH values. On the other hand, experimental studies in transgenic mouse models have shown that treatment with enoxaparin significantly reduces cortical Aβ levels, as well as decreases the number of activated astrocytes around Aβ plaques. However, the interactions between enoxaparin and the ApoE4-Aβ proteins have been poorly explored. In this work, we combine molecular dynamics simulations, molecular docking, and binding free energy calculations to elucidate the molecular properties of the ApoE4-Aβ interactions and the competitive binding affinity of the enoxaparin on the ApoE4 binding sites. In addition, we investigated the effect of the environmental pH levels on those interactions. Our results showed that under different pH conditions, the closed form of the ApoE4 protein, in which the C-terminal domain folds into the protein, remains stabilized by a network of hydrogen bonds. This closed conformation allowed the generation of six different ApoE4-Aβ interaction sites, which were energetically favorable. Systems at pH5 and 6 showed the highest energetic affinity. The enoxaparin molecule was found to have a strong energetic affinity for ApoE4-interacting sites and thus can neutralize or disrupt ApoE4-Aβ complex formation.