Daniela López’s research while affiliated with University of Antioquia and other places

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Publications (1)


Antibacterial activity of the AXOTL-13 peptide on Escherichia coli. (a) Viability percentage after 20 h of growth (endpoint). (b) Viability percentage every hour for 20 h (growth kinetics). C− (N/T): bacteria without treatment. C+ (NaClO): bacteria treated with 0.06% NaClO. C+ (Ramosin): bacteria treated with 40 μM Ramosin peptide. Kinetics data are presented as mean ± SD and endpoint as mean ± SEM. ns: p ≥ 0.005. **: p < 0.01. Blue asterisk: comparison with NaClO; red asterisk: comparison with Ramosin.
Antibacterial activity of the AXOTL-13 peptide on Staphylococcus aureus. (a) Viability percentage after 20 h of growth (endpoint). (b) Viability percentage every hour for 20 h (growth kinetics). C− (N/T): bacteria without treatment. C+ (NaClO): bacteria treated with 0.06% NaClO. C+ (Ramosin): bacteria treated with 40 μM Ramosin peptide. Kinetics data are presented as mean ± SD and endpoint as mean ± SEM. ns: p ≥ 0.005. **: p < 0.01. Blue asterisk: comparison with NaClO; red asterisk: comparison with Ramosin.
Hemolytic activity of AXOTL-13. C+ (Triton X-100): Red blood cells with 0.5% v/v Triton X-100. C− (PBS 1X): Red blood cells with PBS 1X. Data are presented as mean ± SEM. **: p < 0.01. Black asterisk: comparison with Tritón-X-100.
Secondary structure of the AXOTL-13 peptide from Ambystoma mexicanum, modeled by the I-TASSER server. (a) Prediction of amino acids involved in the formation of secondary structures. (b) Three-dimensional model of the secondary structure.
Schiffer–Edmundson wheel representation of the peptide AXOTL-13 from Ambystoma mexicanum simulated by NetWheels tool. Positively charged polar amino acids are shown in green, uncharged polar amino acids in blue, and nonpolar amino acids in purple. The dashed line differentiates the two faces of different polarity; *: isoleucine; **: serine.

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Antibacterial Activity of AXOTL-13, a Novel Peptide Identified from the Transcriptome of the Salamander Ambystoma mexicanum
  • Article
  • Full-text available

November 2024

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88 Reads

Laura Córdoba

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Daniela López

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Mariana Mejía

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[...]

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Laura Medina

Background/Objectives: Antimicrobial peptides are essential molecules in the innate immunity of various organisms and possess a broad spectrum of antimicrobial, antitumor, and immunomodulatory activities. Due to their multifunctionality, they are seen as an alternative for controlling bacterial infections. Although conventional antibiotics have improved health worldwide, their indiscriminate use has led to the emergence of resistant microorganisms. To discover new molecules with antimicrobial activity that could overcome the limitations of traditional antibiotics, this study aimed to identify antimicrobial peptides in Ambystoma mexicanum. Methods: In this study, hypothetical proteins encoded in the Ambystoma mexicanum transcriptome were predicted. These proteins were aligned with peptides reported in the Antimicrobial Peptide Database (APD3) using the Fasta36 program. After identifying peptide sequences with potential antibacterial activity, their expression was confirmed through conventional polymerase chain reaction (PCR) and then chemically synthesized. The antibacterial activity of the synthesized peptides was evaluated against Staphylococcus aureus ATCC 25923 and Escherichia coli ATCC 25922. Results: A new antimicrobial peptide named AXOTL-13 was identified. AXOTL-13 is an amphipathic cationic alpha-helical peptide with the ability to inhibit the growth of Escherichia coli without causing hemolysis in red blood cells, with its action likely directed at the membrane, as suggested by morphological changes observed through scanning electron microscopy. Conclusions: This research is pioneering in evaluating the activity of antimicrobial peptides present in Ambystoma mexicanum and in specifically identifying one of these peptides. The findings will serve as a reference for future research in this field.

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