ArticleProbiotics and antimicrobial proteins2022
Designing Anti-Microbial Peptides Against Major β-Lactamase Enzymes in Clinically Important Gram-Negative Bacterial Pathogens: An In-Silico Study.
Article in Probiotics and antimicrobial proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 27 citations in OpenAlex.
- The Activity of Antimicrobial Peptides (AMPs) Identified Via an Integrated in Silico and Pilot in Vitro Screening Approach Towards ESKAPE Pathogens.Probiotics and antimicrobial proteins · 2026Article
- Promising Future of Engineered Probiotics for Antimicrobial Peptides and Protein Production: Prospects and Industrial Challenges.Probiotics and antimicrobial proteins · 2026Review
- Antimycobacterial peptides as natural therapeutics for tuberculosis: mechanisms and structural features.Frontiers in antibiotics · 2026Review
- From computational screening toFrontiers in microbiology · 2026Article
- Pharmacokinetics Screening, Molecular Docking, and Dynamics Simulations Revealed Novel Antimicrobial Peptide NKLF2 Mutants as Potent Inhibitors of Mycobacterium tuberculosis.Probiotics and antimicrobial proteins · 2026Article
- Novel antimicrobial peptide HFIAP-1 mutant as a β-lactamase inhibitor against extended-spectrum β-lactamases of Escherichia coli: a comprehensive in-silico approach.Archives of microbiology · 2025Article
- Unveiling the potential of antimicrobial peptides to combat Mycobacterium tuberculosis.Archives of microbiology · 2025Review
- Fabrication of a Lipopolysaccharide-Targeting Peptide-Based Colloid for Alleviating Carbapenem-Resistant Enterobacteriaceae-Induced Cutaneous Infection.Advanced healthcare materials · 2025Article
- Article
- Integrating pan-genome and reverse vaccinology to design multi-epitope vaccine against Herpes simplex virus type-1.3 Biotech · 2024Article
- Novel Antimicrobial Peptide SAAP Mutant as a Better Adjuvant to Sulbactam-Based Treatments Against Clinical Strains of XDR Acinetobacter baumannii.Probiotics and antimicrobial proteins · 2024Article
- Antimicrobial Peptides as Immunomodulators and Antimycobacterial Agents to Combat Mycobacterium tuberculosis: a Critical Review.Probiotics and antimicrobial proteins · 2023Review
- Article
- BamA-targeted antimicrobial peptide design for enhanced efficacy and reduced toxicity.Amino acids · 2023Article
- Multi-Epitope Vaccine for Monkeypox Using Pan-Genome and Reverse Vaccinology Approaches.Viruses · 2022Article
- A comprehensive review on genomics, systems biology and structural biology approaches for combating antimicrobial resistance in ESKAPE pathogens: computational tools and recent advancements.World journal of microbiology & biotechnology · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anti-microbial resistance (AMR) creating healthcare concerns worldwide requires ardent exploration of therapeutic alternatives. Although anti-microbial peptides (AMP) are popular for broad-spectrum activity, recent evidence of increasing resistance to membrane-acting AMPs by ESKAPE pathogens has compelled us to design novel AMPs as therapeutic candidates. A library of 60 AMPs comprising natural AMPs and their mutants was constructed through in-silico methods. After physico-chemical property evaluations, each peptide in the library was subjected to flexible molecular docking against four major β-lactamases in Gram-negative ESKAPE pathogens. Among the potent AMP mutants, a Lactoferricin B-Mutant (M4) possessed uniformly high affinity with SHV1, OXA48, NDM1, and AmpC having energies -842.0Kcal/mol, -774.8Kcal/mol, -1103.3Kcal/mol, and -858.8Kcal/mol respectively. Coarse-grained clustering and flexibility analysis further accounted for the residue-level stable configurations of the protein-peptide complexes with high affinity. Highest affinity of Lactoferricin B_M4 was found with NDM1 due to H-bonds, salt-bridges, and hydrophobic interactions with the metallo-β-lactamase domain including crucial active-site residue Asp124. Molecular dynamics simulation further confirmed the stability of Lactoferricin B_M4-NDM1 complex having low residue-level root-mean square deviations (RMSD), atomic-level fluctuations, and radius of gyration (Rg). The study encourages experimental validations and similar methods to identify potential AMPs against drug-resistant pathogens.
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