ArticleProbiotics and antimicrobial proteins2026
Pharmacokinetics Screening, Molecular Docking, and Dynamics Simulations Revealed Novel Antimicrobial Peptide NKLF2 Mutants as Potent Inhibitors of Mycobacterium tuberculosis.
Article in Probiotics and antimicrobial proteins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- Computational screening of antimicrobial peptide analogs targeting AdeB efflux transporter protein in Acinetobacter baumannii associated with multidrug resistance.Scientific reports · 2026Article
- Novel Anti-Microbial Peptides Design and Screening Against the KatG Using Molecular Docking and MD Simulation.Probiotics and antimicrobial proteins · 2026Article
- Synergistic strategies to rescue the last-resort antibiotic colistin.Archives of microbiology · 2026Review
- Review
- A 4-methyl-substituted durlobactam analogue as a potential class-D oxacillinase inhibitor inFrontiers in bioinformatics · 2026Article
- Comparative genomics of carbapenem resistant and susceptible clinicalFrontiers in cellular and infection microbiology · 2026Article
- Biofilm-associated antibiotic tolerance in the era of multidrug resistance: quorum-sensing mechanisms and emerging therapeutic strategies.Frontiers in cellular and infection microbiology · 2026Review
- Machine learning-based virtual screening and density functional theory characterisation of natural inhibitors targeting mutant PBP2x in Streptococcus pneumoniae.Scientific reports · 2025Article
- Peptide-Based Strategies AgainstPharmaceuticals (Basel, Switzerland) · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The increasing threat of multidrug-resistant Mycobacterium tuberculosis (Mtb) underscores the urgent need for novel therapeutics that can circumvent existing resistance mechanisms. The clinical ineffectiveness of current treatment regimens propelled the exploration for alternative antimicrobials with minimal toxicity and multi-target specificity. This study aimed to design and optimize antimicrobial peptides (AMPs) targeting crucial Mtb enzymes, namely, arabinosyltransferase C, DNA gyrase, 30S ribosomal protein S1, and enoyl-[acyl-carrier-protein] reductase. Curated set of 92 natural peptides, exhibiting high positive charge and reported efficacy against Mtb-H37Rv were screened and evaluated for pharmacokinetic properties. To enhance efficacy and overcome the intrinsic limitations of cationic AMPs, a mutant library was generated. Among them, NKLF2 and its mutants (M16C and M16I) demonstrated improved antibacterial efficacy (~ 5%) and favorable pharmacological profiles with no predicted toxicity. Molecular docking revealed enhanced binding affinities of the mutants across multiple targets. Notably, NKLF2_M16I exhibited enhancements of 9.71% and 7.63% in binding affinities against 4NNI and 5VRL respectively, while NKLF2_M16C achieved increments of 5.4% and 4.37% against 4G3N and 3PTY. Intermolecular interaction profiling identified hydrogen bonds, salt bridges, and hydrophobic interactions with the crucial active site residues of each target. Validations through coarse-grained, molecular, and essential dynamics simulations revealed minimal residue-level fluctuations, stable backbone profile, and minimized energy cluster basins ensuring compactness and stability of the protein-peptide docked complexes. These in silico findings open new avenues for further experimental validations and suggest that NKLF2 mutants in combination with conventional anti-TB drugs could pave the path towards the development of effective therapeutics in combating Mtb.
Indexed as
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.