Integrating Docking, Dynamics, and Assays to Predict Antimicrobial Peptide Interactions with Mycolic Acid Membranes in Mycobacterium tuberculosis.

Roque-Borda, Cesar Augusto et al.·ACS measurement science au·2025·lowcomputational
RPEP-13304Computationallow2025RETHINKTHC RESEARCH DATABASErethinkthc.com/research

Quick Facts

Study Type
computational
Evidence
low
Sample
N=Not applicable (computational/lab study)
Participants
M. tuberculosis and model bacterial membranes

What This Study Found

A tryptophan-modified amphibian antimicrobial peptide (W-B1CTcu5) showed potent activity against M. tuberculosis (MIC 3.2 micrograms/mL) with strong membrane interaction and multitarget binding, though hemolytic toxicity remains a concern.

Key Numbers

W-B1CTcu5 MIC = 3.2 micrograms/mL against M. tuberculosis. Targets MspA, CpnT, and Ag85B proteins. Low RMSD and residue fluctuation correlated with antimicrobial activity. Hemolytic activity noted.

How They Did This

Comparative evaluation of four B1CTcu5 analogs. Experimental MIC testing against MTB. Molecular dynamics simulations of membrane interaction. Docking against key MTB proteins.

Why This Research Matters

This study combines lab testing with molecular simulations to understand why some peptide modifications improve TB-killing ability. The approach could accelerate design of less toxic anti-TB peptides.

What This Study Doesn't Tell Us

Hemolytic toxicity limits clinical potential. In vitro activity only. Simulations may not fully predict in vivo behavior. Single parent peptide scaffold. No animal testing.

Trust & Context

Original Title:
Integrating Docking, Dynamics, and Assays to Predict Antimicrobial Peptide Interactions with Mycolic Acid Membranes in Mycobacterium tuberculosis.
Published In:
ACS measurement science au, 5(6), 981-1000 (2025)
Database ID:
RPEP-13304

Evidence Hierarchy

Meta-Analysis / Systematic Review
Randomized Controlled Trial
Cohort / Case-Control
Cross-Sectional / ObservationalSnapshot without intervening
This study
Case Report / Animal Study
What do these levels mean? →

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Cite This Study

RPEP-13304·https://rethinkpeptides.com/research/RPEP-13304

APA

Roque-Borda, Cesar Augusto; Ramirez Delgado, Oswaldo Julio; Duran Gleriani Primo, Laura Maria; Dyhr, Emma; Sæbø, Ingvill Pedersen; Helgesen, Emily; Booth, James; Franzyk, Henrik; Hansen, Paul R; Morales-Navarrete, Hernan; de la Torre, Beatriz G; Albericio, Fernando; Perdigão, João; Pavan, Fernando Rogério. (2025). Integrating Docking, Dynamics, and Assays to Predict Antimicrobial Peptide Interactions with Mycolic Acid Membranes in Mycobacterium tuberculosis.. ACS measurement science au, 5(6), 981-1000. https://doi.org/10.1021/acsmeasuresciau.5c00126

MLA

Roque-Borda, Cesar Augusto, et al. "Integrating Docking, Dynamics, and Assays to Predict Antimicrobial Peptide Interactions with Mycolic Acid Membranes in Mycobacterium tuberculosis.." ACS measurement science au, 2025. https://doi.org/10.1021/acsmeasuresciau.5c00126

RethinkPeptides

RethinkPeptides Research Database. "Integrating Docking, Dynamics, and Assays to Predict Antimic..." RPEP-13304. Retrieved from https://rethinkpeptides.com/research/roque-borda-2025-integrating-docking-dynamics-and

Access the Original Study

Study data sourced from PubMed, a service of the U.S. National Library of Medicine, National Institutes of Health.

This study breakdown was produced by the RethinkPeptides research team. We analyze and report published research findings without making health recommendations. All interpretations are based solely on the published abstract and study data.