Antimicrobial peptides (the alternate plural tag) covers the same field as #antimicrobial-peptide. Coverage runs across Peptilogics' biofilm work, Fedora's FPI-2119 lactivicin, Longhorn Vaccines' DRG5-BD11, and the HMD-AMP discovery platform from HLB Innovation.
The academic side has been productive. Groups at Birmingham (PEPITEM), Oxford, and others have published on AMP discovery, MRSA, and biofilm penetration. Nature Biomedical Engineering and Nature Biotechnology AMP papers continue to surface AI-discovered scaffolds.
For the singular form, see #antimicrobial-peptide. For the policy and resistance context, see #amr and #antibiotic-resistance.
Researchers at the Hebrew University of Jerusalem designed melittin derivatives and ran experimental evolution tests in Staphylococcus aureus: full-length melittin and highly hydrophobic variants drew high resistance, while the truncated Mel(5-24) kept its antibacterial activity with minimal resistance and less cross-resistance to other peptides. Melittin-evolved bacteria shared mutations in pmtR, while Mel(5-24)-evolved bacteria changed only ydbT, and resistance tracked with peptide hydrophobicity and length, the Antimicrobial Agents and Chemotherapy paper reports. The work was done in lab cultures.
In a double-blind controlled trial at the First Affiliated Hospital of Chongqing Medical University, 52 patients with chronic lip inflammation used a lip balm containing calcium-based antimicrobial peptide compounds or 0.03% tacrolimus ointment for four weeks. Both groups improved markedly by week 4, though tacrolimus worked faster at week 2; mild adverse events occurred in 7.7% vs. 23.1%, and 45 patients completed treatment, the Journal of Cosmetic Dermatology paper reports.
Konkuk University researchers modeled antimicrobial peptides on a Mycobacterium tuberculosis enzyme, adenylate kinase, that recognizes both Gram-negative and Gram-positive cell-wall molecules, then added non-natural amino acids, an N-terminal fatty acid chain, and an arginine extension. The lead peptide, YK-mAK-17, killed carbapenem-resistant Acinetobacter baumannii and MRSA quickly by disrupting their membranes, showed little resistance development, and improved survival and reduced organ damage in mice with septic shock caused by either bacterium, the Journal of Medicinal Chemistry paper reports.
Researchers at Henan Institute of Science and Technology screened porcine cathelicidin peptides against porcine reproductive and respiratory syndrome virus, which vaccines control poorly, and found that GI24, the first 24 amino acids of PMAP-36, blocked the virus from attaching to and entering cells. GI24 also reduced inflammatory signaling triggered by the virus and by bacterial endotoxin, working through the TREM1 gene, the Virology paper reports. The tests were done in cells only.
Researchers at Rzeszów University of Technology, with colleagues in Gdańsk, Kraków, and Ljubljana, built AMPAB5 from cobra (Naja ashei) venom factor sequences. Against Pseudomonas aeruginosa, which resists chloramphenicol (MIC 250 μg/mL), combining the two cut the MICs to 15.63 μg/mL for the antibiotic and 5.86 μg/mL for the peptide; AMPAB5 also blocked and cleared biofilms, modulated IL-1β and TNF-α release by human macrophages, and showed no hemolysis or toxicity to skin or Caco-2 cells, the Toxicology and Applied Pharmacology paper reports. The work was done in cells only, and two authors hold a patent assigned to the university.
Leeds Teaching Hospitals enrolled the first patient outside the U.S. in RETAIN (NCT07214311), a randomized, double-blind, placebo-controlled Phase 2/3 trial of zaloganan (PLG0206) in people having their infected knee implant cleaned and kept in place rather than replaced. The trial plans about 240 patients at 50 sites in the U.S., U.K., and Australia, with treatment failure within 12 months as its primary endpoint. Peptilogics says one of 13 patients had a recurrence in its open-label Phase 1b study, compared with published 12-month failure rates of 35% to 55% under standard care, a comparison across different studies.
Researchers at Anhui University and a Guangdong marine science lab designed two derivatives of the antimicrobial peptide MAP 34-B. MAP 34B-1 was more active against E. coli and the drug-resistant hospital pathogen Acinetobacter baumannii, cut bacterial viability within two hours by disrupting membranes, kept working under the salt and heat conditions tested, and caused less damage to mammalian cells and red blood cells than MAP 34B-2, the Journal of Peptide Science paper reports. The work was done in cell cultures only.
Xiamen University researchers synthesized Sparadin118–140, a 23-residue helical peptide from the mud crab Scylla paramamosain, and found it killed three Pseudomonas species by disrupting their membranes, kept working at refrigeration temperature, and broke up biofilms. It also dampened inflammation caused by P. aeruginosa lipopolysaccharide in macrophages and zebrafish. On refrigerated tilapia fillets it slowed bacterial growth and spoilage about as well as the preservative potassium sorbate, according to the Journal of Agricultural and Food Chemistry paper.
Researchers at Aix-Marseille University and the French armed forces biomedical research institute (IRBA) made versions of the Lynronne antimicrobial peptides in which every positively charged residue was histidine, lysine, or arginine, reporting in the Journal of Peptide Science. All-histidine versions were inactive, all-lysine versions were most potent against Gram-negative bacteria, especially E. coli, and all-arginine versions were more active against Gram-positive bacteria and more stable in salt or serum but damaged more red blood cells. Lynronne-3 and its all-lysine variant were best at preventing and clearing biofilms; the work was in lab tests only.
Researchers fused residues 13 to 36 of the human antimicrobial peptide LL-37 with thymopentin (TP5), a five-amino-acid immune peptide, and produced the hybrid in Pichia pastoris yeast at about 20.5 mg per liter and 95.2% purity, reporting in Frontiers in Pharmacology. LL37-TP5 killed Gram-negative and Gram-positive poultry pathogens at low concentrations, neutralized bacterial endotoxin, cut nitric oxide, IL-6, TNF-α, and IL-1β in stimulated mouse macrophages, and was less toxic to cells and red blood cells than LL-37. The tests were in the lab, with poultry farming as the intended use.
Using NMR spectroscopy, docking, and simulations, researchers reported in Communications Chemistry that the antimicrobial peptide thanatin binds beside the catalytic groove of NDM-1, an enzyme that lets bacteria destroy carbapenem antibiotics, and inhibits it by restricting a flexible loop while both zinc ions stay bound. In bacterial assays the effect partly restored carbapenem sensitivity, cutting viable cell output by 50% even with high enzyme levels. The work is lab-only.
The Database of Antimicrobial Activity and Structure of Peptides, curated at the Ivane Beritashvili Center of Experimental Biomedicine in Tbilisi with NIAID collaborators, released version 4, described in Nucleic Acids Research. It now holds more than 25,000 entries linking peptides to measured antimicrobial, antibiofilm, anticancer, and toxicity results under stated test conditions, and adds SMILES chemical structures, synergy records, and more than 9,200 molecular-dynamics simulations to help train prediction models.
Wayne State University School of Medicine researchers tested recombinant human thymosin beta-4, the protein that TB-500 is derived from, against a laboratory Staphylococcus aureus strain and two clinical isolates, reporting in Microbiology Spectrum. Alone it had little direct antibacterial activity even at high concentrations, but it acted synergistically with several of the four antibiotics tested (moxifloxacin, ciprofloxacin, oxacillin, vancomycin), mainly against free-floating bacteria. It did little against established biofilms, and all of the work was in lab dishes.
Princeton University chemists reported in ACS Chemical Biology on October 27, 2026 that conjugating a cell-penetrating peptide to the loop of the lasso peptides citrocin and microcin J25, which kill bacteria by blocking RNA polymerase but depend on specific transporters to get inside, gave them activity against all four Gram-negative ESKAPE pathogens. The conjugates were more potent than the parent peptides, with minimum inhibitory concentrations from high nanomolar to single micromolar, and entered E. coli through both transporter-dependent and transporter-independent routes, which the authors say could limit one path to resistance. The work is in bacterial cultures.
Researchers at Aarhus University's Department of Biological and Chemical Engineering reported in The Journal of Antibiotics on October 26, 2026 that the follower peptide attached to triculamin's precursor, a feature unlike other lasso peptides, is essential for making the antibiotic. Structural predictions and targeted mutations suggest the follower binds the ring-closing enzyme and delivers the core peptide to its active site. The team made triculamin analogs by changing the core peptide, identified lysine-3 in the ring as the acetylation site, and found Burkholderia sp. FERM BP-3421 to be a better host for producing it.
Researchers at the Federal University of Mato Grosso do Sul in Brazil reported in Probiotics and Antimicrobial Proteins on October 24, 2026 that FK18, a rationally designed cationic peptide, inhibited Candida and Cryptococcus species at 5 to more than 40 µM, and at 10 µM eliminated Candida tropicalis cells within four hours. It rapidly permeabilized fungal membranes, its activity fell four-fold when extra ergosterol was added, and checkerboard tests showed strong synergy with the antifungal fluconazole. NMR showed FK18 forms a stable amphipathic helix in membrane-like environments; all results are from lab tests and simulations.
Researchers from the Chinese Academy of Sciences' Xinjiang Institute of Ecology and Geography and the Chinese Academy of Medical Sciences reported in ACS Omega on October 23, 2026 that NA-CATH, a cathelicidin peptide first found in the Chinese cobra, was the best of five antimicrobial peptides tested on clinical multidrug-resistant Klebsiella pneumoniae and Acinetobacter baumannii in the lab, but killed all treated wax moth larvae. Screening nearly 50,000 computer-designed variants produced NA-7, which kept antibacterial activity, improved survival of Klebsiella-infected larvae compared with the parent peptide, and caused lower acute toxicity and fewer kidney changes in mice. The work is preclinical.
Researchers at Mexico's Ensenada Center for Scientific Research and Higher Education (CICESE) reported in the Journal of Applied Microbiology on October 22, 2026 that of four machine-learning-selected peptides, one called P2 had the best activity profile. It inhibited two Candida albicans reference strains and a C. parapsilosis clinical isolate at 62.5 µM, while C. glabrata needed 250 µM, and it still killed bacteria after 15 minutes at 100°C. Hemolysis reached 12% at 500 µM, and human 293T cells were unaffected up to 50 µM but badly damaged at 500 µM; the work is in lab cultures only.