Publications by authors named "R Garduno-Juarez"

Amyloid-β (Aβ) peptides aggregated into plaques deposited in the brain are the main hallmark of Alzheimer's disease (AD), a social and economic burden worldwide. In this context, insoluble Aβ fibrils are the main components of plaques. The recent trials that used approved AD drugs show that they can remove the fibrils from AD patients' brains, but they did not halt the course of the disease.

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Article Synopsis
  • Computational modeling (CM) is a valuable method for analyzing complex systems like biopolymers in biomedical engineering, predicting experiment results, and speeding up scientific progress.
  • Key areas of CM in biopolymer research include Computer-aided design (CAD/CAM) for creating detailed 3D models, finite element analysis for studying mechanical properties, and molecular dynamics (MD) simulations for understanding molecular behavior.
  • The integration of in silico and in vitro experiments in CM enhances research efficiency and reduces costs, marking a growing trend in biomedical engineering fields.
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Calcium ion regulation plays a crucial role in maintaining neuronal functions such as neurotransmitter release and synaptic plasticity. Copper (Cu ) coordination to amyloid-β (Aβ) has accelerated Aβ aggregation that can trigger calcium dysregulation by enhancing the influx of calcium ions by extensive perturbing integrity of the membranes. Aβ aggregation, calcium dysregulation, and membrane damage are Alzheimer disease (AD) implications.

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Discrepin is a 38-residue α-toxin extracted from the venom of the Venezuelan scorpion , which inhibits ionic transit in the voltage-dependent potassium channels (Kv) of A-type current. The effect of specific residues on the IC between Discrepine and Kv4.3, the main component of A-type currents, is known; however, the molecular details of the toxin-channel interaction are not known.

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Article Synopsis
  • Ascaphins are promising cationic antimicrobial peptides with potential against multidrug-resistant pathogens, but their molecular target and mechanism are still unclear.
  • Research using simulations and biophysical methods revealed that ascaphin-8 is an alpha-helical peptide that interacts with bacterial membranes, causing leakage and altering fluidity.
  • Variants of ascaphin-8 showed high activity on bacterial membranes but diminished effectiveness on sterol-rich membranes, suggesting specificity for bacterial targets and highlighting their potential in combating MDR infections.
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