Research graph
References from Biomedical Applications of Antimicrobial Peptides: Multifunctional Mechanisms, Engineering Strategies, and Therapeutic Development. Local targets link to admitted publications; unresolved targets remain external evidence.
Molecular mechanism of action, resistance to antibiotics and modern approaches: an overview
10.1016/j.microb.2025.100502 · 2025 · External reference
Clinically relevant mutations in core metabolic genes confer antibiotic resistance
10.1126/science.aba0862 · 2021 · External reference
Comparative effectiveness of switching to daptomycin versus remaining on vancomycin among patients with methicillin-resistant Staphylococcus aureus (MRSA) bloodstream infections
10.1093/cid/ciaa1572 · 2021 · External reference
Identification of daptomycin-binding proteins in the membrane of Enterococcus hirae
10.1128/aac.39.9.2068 · 1995 · External reference
Rotational-echo double resonance characterization of the effects of vancomycin on cell wall synthesis in Staphylococcus aureus
10.1021/bi0202326 · 2002 · External reference
Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications
10.1016/s0734-9750(03)00077-6 · 2003 · External reference
Antimicrobial peptides of multicellular organisms
10.1038/415389a · 2002 · External reference
Studies on a bactericidal agent extracted from a soil Bacillus : II. Protective effect of the bactericidal agent against experimental pneumococcus infections in mice
10.1084/jem.70.1.11 · 1939 · External reference
The production of bactericidal substances by aerobic sporulating Bacilli
10.1084/jem.73.5.629 · 1941 · External reference
‘Aerosporin’, an antibiotic produced by Bacillus aerosporus Greer
10.1038/160263a0 · 1947 · External reference
Defensins. Natural peptide antibiotics of human neutrophils
10.1172/jci112120 · 1985 · External reference
How membrane-active peptides get into lipid membranes
10.1021/acs.accounts.6b00074 · 2016 · External reference
The role of bacterial lipid diversity and membrane properties in modulating antimicrobial peptide activity and drug resistance
10.1016/j.cbpa.2019.05.025 · 2019 · External reference
Antimicrobial peptides at (lipid) interfaces: insights from monolayer models
10.1016/j.cis.2025.103775 · 2026 · External reference
Unveiling mechanisms of antimicrobial peptide: actions beyond the membranes disruption
2024 · External reference
The bioprospecting of microbial-derived antimicrobial peptides for sustainable agriculture
10.1016/j.eng.2022.08.011 · 2023 · External reference
Diversity of aquatic Pseudomonas species and their activity against the fish pathogenic oomycete Saprolegnia
2015 · External reference
Gill amoebae from freshwater rainbow trout (Oncorhynchus mykiss): in vitro evaluation of antiparasitic compounds against Vannella sp
10.1111/jfd.13162 · 2020 · External reference
Impact of Pseudomonas H6 surfactant on all external life cycle stages of the fish parasitic ciliate Ichthyophthirius multifiliis
10.1111/jfd.12810 · 2018 · External reference
Effects of a Pseudomonas H6 surfactant on rainbow trout and Ichthyophthirius multifiliis: in vivo exposure
10.1016/j.aquaculture.2021.737479 · 2022 · External reference
Anticancer activities of natural antimicrobial peptides from animals
2023 · External reference
Playing with biological selectivity: antimicrobial peptides and bacteriophages-based optical biosensors for pathogenic bacteria detection
10.1016/j.trac.2024.117565 · 2024 · External reference
Advances in antimicrobial peptides for food systems: a review of applications, species-specific targets, and strategies to enhance specificity
10.1016/j.tifs.2025.105348 · 2025 · External reference
AI-driven antimicrobial peptide discovery: mining and generation
2025 · External reference
Molecular design drives nanoarchitecture in self-assembling antimicrobial peptides
10.1016/j.tibs.2025.08.003 · 2025 · External reference
AI-guided design of antimicrobial peptide hydrogels for precise treatment of drug-resistant bacterial infections
10.1002/adma.202500043 · 2025 · External reference
The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms
10.1126/scitranslmed.aan4044 · 2018 · External reference
Correlation between hemolytic activity, cytotoxicity and systemic in vivo toxicity of synthetic antimicrobial peptides
10.1038/s41598-020-69995-9 · 2020 · External reference
Antimicrobial peptides towards clinical application: delivery and formulation
10.1016/j.addr.2021.05.028 · 2021 · External reference
Antimicrobial peptides: structure, functions and translational applications
10.1038/s41579-025-01200-y · 2025 · External reference
Biosynthesis of antimicrobial peptides and its medical application
2022 · External reference
Peptide head-to-tail cyclization: a “Molecular Claw” approach
10.1002/ejoc.202100185 · 2021 · External reference
AI-based D-amino acid substitution for optimizing antimicrobial peptides to treat multidrug-resistant bacterial infection
2026 · External reference
Advanced delivery systems for peptide antibiotics
10.1016/j.addr.2023.114733 · 2023 · External reference
Review on microbial recombination expression of antimicrobial peptides
10.1016/j.cej.2025.170733 · 2025 · External reference
Embracing the era of antimicrobial peptides with marine organisms
10.1039/d3np00031a · 2024 · External reference
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
10.1016/j.bbamem.2006.03.030 · 2006 · External reference
Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide
10.1016/j.peptides.2019.170106 · 2019 · External reference
Cathelin-related antimicrobial peptide differentially regulates T- and B-cell function
10.1002/eji.201141606 · 2011 · External reference
Cathelicidin AS-12W derived from the Alligator sinensis and its antimicrobial activity against drug-resistant Gram-negative bacteria in vitro and in vivo
10.1007/s12602-024-10250-2 · 2025 · External reference
The neutrophil antimicrobial peptide cathelicidin promotes Th17 differentiation
10.1038/s41467-021-21533-5 · 2021 · External reference
Increased LL-37 in psoriasis and other inflammatory disorders promotes LDL uptake and atherosclerosis
10.1172/jci172578 · 2024 · External reference
Cathelicidin LL-37-ApoB-100 interaction promotes LDL clearance and attenuates cholesterol accumulation in the liver
10.1007/s11427-025-3006-2 · 2026 · External reference
Decoding LL-37: structure and antimicrobial mechanisms against microbial threats
10.1016/j.meegid.2025.105853 · 2025 · External reference
Transmembrane pores formed by human antimicrobial peptide LL-37
10.1016/j.bpj.2011.02.018 · 2011 · External reference
Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
10.1128/aac.42.9.2206 · 1998 · External reference
Antimicrobial peptides for combating drug-resistant bacterial infections
10.1016/j.drup.2023.100954 · 2023 · External reference
Serine protease HtrA promotes Campylobacter jejuni intestinal colonization through degrading antimicrobial peptide LL-37
2026 · External reference
Trematocine, a novel antimicrobial peptide from the Antarctic fish Trematomus bernacchii: identification and biological activity
10.3390/antibiotics9020066 · 2020 · External reference
Antibacterial and antiparasitic activities analysis of a hepcidin-like antimicrobial peptide from Larimichthys crocea
10.1007/s13131-020-1580-6 · 2020 · External reference
β-defensin from the Asian sea bass, Lates calcarifer: molecular prediction and phylogenetic analysis
10.1007/s12602-021-09804-5 · 2021 · External reference
Induced expression of cathelicidins in trout (Oncorhynchus mykiss) challenged with four different bacterial pathogens
10.1002/psc.3089 · 2018 · External reference
Identification of a novel cathelicidin gene in the rainbow trout, Oncorhynchus mykiss
10.1128/iai.73.8.5053-5064.2005 · 2005 · External reference
Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.)
10.1016/s1570-9639(03)00018-9 · 2003 · External reference
Modular analysis of hipposin, a histone-derived antimicrobial peptide consisting of membrane translocating and membrane permeabilizing fragments
10.1016/j.bbamem.2014.04.010 · 2014 · External reference
Regulators and signalling in insect antimicrobial innate immunity: functional molecules and cellular pathways
10.1016/j.cellsig.2021.110003 · 2021 · External reference
Thanatin: a promising antimicrobial peptide targeting the Achilles’ heel of multidrug-resistant bacteria
10.3390/ijms25179496 · 2024 · External reference
Dietary influence on growth, physicochemical stability, and antimicrobial mechanisms of antimicrobial peptides in black soldier fly larvae
10.3390/insects15110872 · 2024 · External reference
Discovery and characterization of a novel Lepidoptera-specific antimicrobial peptide from the fall armyworm, Spodoptera frugiperda (Lepidoptera: Noctuidae)
10.1111/1744-7917.13471 · 2025 · External reference
Cathelicidin-DM is an antimicrobial peptide from Duttaphrynus melanostictus and has wound-healing therapeutic potential
10.1021/acsomega.0c00189 · 2020 · External reference
Temporin A and its retro-analogues: synthesis, conformational analysis and antimicrobial activities
10.1002/psc.762 · 2006 · External reference
Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs
10.1021/pr200782u · 2011 · External reference
Diversity and molecular evolution of antimicrobial peptides in caecilian amphibians
10.3390/toxins16030150 · 2024 · External reference
Metal ions provide structural stability and compactness to tetrameric purothionin
10.1039/c6ra16576a · 2016 · External reference
Mechanism of β-purothionin antimicrobial peptide inhibition by metal ions: molecular dynamics simulation study
10.1016/j.bpc.2005.12.004 · 2006 · External reference
The identification of leaf thionin as one of the main jasmonate-induced proteins of barley (Hordeum vulgare)
10.1007/bf00027341 · 1992 · External reference
Antimicrobial peptides from plants
10.3390/ph8040711 · 2015 · External reference
Research advances on the structure, function and regulation of defensins gene family in plants
2018 · External reference
Lipid transfer proteins: structure, classification and prospects of genetic engineering for improved disease resistance in plants
10.1007/s11240-023-02445-2 · 2023 · External reference
Hevein-like antimicrobial peptides of plants
10.1134/s0006297917130065 · 2017 · External reference
Snakin-1, a peptide from potato that is active against plant pathogens
10.1094/mpmi.1999.12.1.16 · 1999 · External reference
A plant peptide with dual activity against multidrug-resistant bacterial and fungal pathogens
10.1126/sciadv.adt8239 · 2025 · External reference
A multifunctional citrus-derived antimicrobial peptide controls vascular bacterial pathogens
10.1111/jipb.70057 · 2025 · External reference
Efficient in planta production of amidated antimicrobial peptides that are active against drug-resistant ESKAPE pathogens
10.1038/s41467-023-37003-z · 2023 · External reference
Bacteriocin diversity, function, discovery and application as antimicrobials
10.1038/s41579-024-01045-x · 2024 · External reference
Mining, heterologous expression, purification, antibactericidal mechanism, and application of bacteriocins: a review
10.1111/1541-4337.12658 · 2021 · External reference
Bacterial peptide antibiotics: a comprehensive review on biosynthesis, mechanisms, and therapeutic potential
10.1016/j.nexres.2025.100850 · 2025 · External reference
Bacteriocins: classification, synthesis, mechanism of action and resistance development in food spoilage causing bacteria
10.1016/j.micpath.2019.01.002 · 2019 · External reference
Toward safer and sustainable food preservation: a comprehensive review of bacteriocins in the food industry
10.1042/bsr20241594 · 2025 · External reference
The clinical praxis of bacteriocins as natural anti-microbial therapeutics
10.1007/s00203-024-04152-8 · 2024 · External reference
Uncovering the arsenal of class II bacteriocins in salivarius streptococci
10.1038/s42003-024-07217-y · 2024 · External reference
The progress of the biotechnological production of class IIa bacteriocins in various cell factories and its future challenges
10.3390/ijms25115791 · 2024 · External reference
Circular and leaderless bacteriocins: biosynthesis, mode of action, applications, and prospects
10.3389/fmicb.2018.02085 · 2018 · External reference
Some chemical and physical properties of nisin, a small-protein antibiotic produced by Lactococcus lactis
10.1128/aem.56.8.2551-2558.1990 · 1990 · External reference
The lantibiotic nisin induces lipid II aggregation, causing membrane instability and vesicle budding
10.1016/j.bpj.2015.01.020 · 2015 · External reference
Inhibition of Listeria monocytogenes by food antimicrobials applied singly and in combination
10.1111/j.1750-3841.2010.01843.x · 2010 · External reference
Effects of nisin loaded chitosan-pectin nanoparticles on shelf life and storage stability of room temperature stored processed cheese
10.1016/j.foodchem.2025.143103 · 2025 · External reference
Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria
2007 · External reference
Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
10.1128/jb.174.22.7428-7435.1992 · 1992 · External reference
Review on current status of echinocandins use
10.3390/antibiotics9050227 · 2020 · External reference
Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus
10.1038/nature04051 · 2005 · External reference
Development and research progress of microalgae as a production platform for antimicrobial peptides
10.1007/s10811-025-03472-6 · 2025 · External reference
Multimer of the antimicrobial peptide Mytichitin-A expressed in Chlamydomonas reinhardtii exerts a broader antibacterial spectrum and increased potency
10.1016/j.jbiosc.2017.08.021 · 2018 · External reference
Antibacterial efficacy of Chlamydomonas reinhardtii-expressed Enterocin RM6 against Gram-positive and Gram-negative bacteria
10.1007/s12602-025-10641-z · 2026 · External reference
Expression of tandem repeat cecropin B in Chlamydomonas reinhardtii and its antibacterial effect
10.3724/sp.j.1206.2010.00671 · 2012 · External reference
Precise construction of an antimicrobial peptide targeting bacterial cell membranes derived from natural peptides
2026 · External reference
Frog-derived synthetic peptides display anti-infective activity against Gram-negative pathogens
10.1016/j.tibtech.2025.02.007 · 2025 · External reference
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
10.1016/s0006-3495(03)70031-9 · 2003 · External reference
Antimicrobial peptides under clinical investigation
10.1002/pep2.24122 · 2019 · External reference
In silico-based design of a hybrid peptide with antimicrobial activity against multidrug-resistant Pseudomonas aeruginosa using a spider toxin peptide
10.3390/toxins15120668 · 2023 · External reference
LL-37: structures, antimicrobial activity, and influence on amyloid-related diseases
10.3390/biom14030320 · 2024 · External reference
Temporins: multifunctional peptides from frog skin
10.3390/ijms24065426 · 2023 · External reference
The pearl jubilee of microcin J25: thirty years of research on an exceptional lasso peptide
10.1039/d3np00046j · 2024 · External reference
Mechanism-driven screening of membrane-targeting and pore-forming antimicrobial peptides
2026 · External reference
Mimics of host defense peptides derived from dendronized polylysines for antibacterial and anticancer therapy
10.1021/acsmacrolett.4c00187 · 2024 · External reference
Identification of potent antimicrobial peptides via a machine-learning pipeline that mines the entire space of peptide sequences
10.1038/s41551-022-00991-2 · 2023 · External reference
A generative artificial intelligence approach for the discovery of antimicrobial peptides against multidrug-resistant bacteria
10.1038/s41564-025-02114-4 · 2025 · External reference
Antibacterial mechanism of action of arylamide foldamers
10.1128/aac.05009-11 · 2011 · External reference
Self-assembling and pore-forming peptoids as antimicrobial biomaterials
10.1021/acsnano.4c05250 · 2024 · External reference
De novo design of antimicrobial polymers, foldamers, and small molecules: from discovery to practical applications
10.1021/ar900036b · 2010 · External reference
Advances in the discovery, mechanism of action, optimization of activity and potential for clinical application of antimicrobial peptides
10.1016/j.cej.2024.158962 · 2025 · External reference
Development of aromatic-linked diamino acid antimicrobial peptide mimics with low hemolytic toxicity and excellent activity against methicillin-resistant Staphylococcus aureus (MRSA)
10.1021/acs.jmedchem.2c01583 · 2023 · External reference
Main-chain cationic bile acid polymers mimicking facially amphiphilic antimicrobial peptides
10.1021/acsami.3c06424 · 2023 · External reference
New strategies for novel antibiotics: peptides targeting bacterial cell membranes
10.4149/gpb_2009_02_105 · 2009 · External reference
Advances in antimicrobial peptides: from mechanistic insights to chemical modifications
10.1016/j.biotechadv.2025.108570 · 2025 · External reference
Advances in antimicrobial peptides: mechanisms, design innovations, and biomedical potential
10.3390/molecules30071529 · 2025 · External reference
Barrel-stave model or toroidal model? A case study on Melittin pores
10.1016/s0006-3495(01)75802-x · 2001 · External reference
Structure of the Alamethicin pore reconstructed by X-ray diffraction analysis
10.1529/biophysj.107.126474 · 2008 · External reference
Interaction of Alamethicin with ether-linked phospholipid bilayers: oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies
10.1529/biophysj.105.067678 · 2005 · External reference
Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy
10.1529/biophysj.108.136242 · 2009 · External reference
Antimicrobial peptides targeting Gram-positive bacteria
10.3390/ph9030059 · 2016 · External reference
Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly
2025 · External reference
Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices
10.1038/s41467-025-62604-1 · 2025 · External reference
Membrane active peptides and their biophysical characterization
10.3390/biom8030077 · 2018 · External reference
Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain
10.1021/bi802025a · 2008 · External reference
Biophysical investigations elucidating the mechanisms of action of antimicrobial peptides and their synergism
10.3390/biom8020018 · 2018 · External reference
How lipids influence the mode of action of membrane-active peptides
10.1016/j.bbamem.2007.06.015 · 2007 · External reference
Interaction of LL-37 human cathelicidin peptide with a model microbial-like lipid membrane
10.1016/j.bioelechem.2021.107842 · 2021 · External reference
Antimicrobial peptides: mechanism of action, activity and clinical potential
2021 · External reference
Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin
10.1007/s002329900201 · 1997 · External reference
Membrane pores induced by magainin
10.1021/bi9620621 · 1996 · External reference
Cooperative antimicrobial action of melittin on lipid membranes: a coarse-grained molecular dynamics study
10.1016/j.bbamem.2022.183955 · 2022 · External reference
Melittin-induced permeabilization, re-sealing, and re-permeabilization of E.coli membranes
10.1016/j.bpj.2017.10.046 · 2018 · External reference
Bacterial membrane lipids: diversity in structures and pathways
10.1093/femsre/fuv008 · 2016 · External reference
Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
10.1038/nrmicro1861 · 2008 · External reference
Gram-positive bacterial cell envelopes: the impact on the activity of antimicrobial peptides
10.1016/j.bbamem.2015.11.004 · 2016 · External reference
The power of asymmetry: architecture and assembly of the Gram-negative outer membrane lipid bilayer
10.1146/annurev-micro-102215-095308 · 2016 · External reference
The bacterial outer membrane as a drug barrier
10.1016/s0966-842x(97)81773-8 · 1997 · External reference
Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism
10.1038/s41564-024-01696-9 · 2024 · External reference
Lipid II as a target for antibiotics
10.1038/nrd2004 · 2006 · External reference
Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
10.1073/pnas.0605079103 · 2006 · External reference
Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state NMR
10.1021/bi101975v · 2011 · External reference
Wall teichoic acids are direct molecular targets of antimicrobial peptides in Gram-positive bacteria
10.1021/jacs.5c18971 · 2026 · External reference
Peptide antibiotics
10.1016/s0140-6736(97)80051-7 · 1997 · External reference
Antimicrobial peptides: current status, mechanisms of action, and strategies to overcome therapeutic limitations
10.3390/microorganisms13112574 · 2025 · External reference
Antimicrobial peptide activity is anticorrelated with lipid A leaflet affinity
10.1371/journal.pone.0242907 · 2020 · External reference
Outer-membrane permeabilization, LPS transport inhibition: activity, interactions, and structures of thanatin derived antimicrobial peptides
10.3390/ijms25042122 · 2024 · External reference
The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 β-hairpin region in the recognition mechanism
10.1042/bj20042107 · 2005 · External reference
Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin
10.1073/pnas.1817352116 · 2019 · External reference
Focal targeting of the bacterial envelope by antimicrobial peptides
10.3389/fcell.2016.00055 · 2016 · External reference
Quaternized antimicrobial peptide mimics based on harmane as potent anti-MRSA agents by multi-target mechanism covering cell wall, cell membrane and intracellular targets
10.1016/j.ejmech.2024.116657 · 2024 · External reference
Antifungal peptides from living organisms
10.3389/fmicb.2024.1511461 · 2024 · External reference
Repositioning antimicrobial peptides against WHO-priority fungi
10.1002/advs.202509567 · 2025 · External reference
Antimicrobial peptides: structure, mechanism, and modification
10.1016/j.ejmech.2023.115377 · 2023 · External reference
Non-lytic antibacterial peptides that translocate through bacterial membranes to act on intracellular targets
10.3390/ijms20194877 · 2019 · External reference
Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II
10.1016/j.febslet.2008.04.036 · 2008 · External reference
Targeting nucleic acid phase transitions as a mechanism of action for antimicrobial peptides
10.1038/s41467-023-42374-4 · 2023 · External reference
Aggregation-prone antimicrobial peptides target gram-negative bacterial nucleic acids and protein synthesis
10.1016/j.actbio.2024.12.002 · 2025 · External reference
The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin
10.1038/nsmb.3031 · 2015 · External reference
Inhibition of translation termination by the antimicrobial peptide drosocin
10.1038/s41589-023-01300-x · 2023 · External reference
Proline-rich antimicrobial peptides targeting protein synthesis
10.1039/c7np00020k · 2017 · External reference
The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17)
10.1093/nar/gkaf324 · 2025 · External reference
The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding
10.1038/s41467-025-55836-8 · 2025 · External reference
Rumicidins are a family of mammalian host-defense peptides plugging the 70S ribosome exit tunnel
10.1038/s41467-024-53309-y · 2024 · External reference
A broad-spectrum lasso peptide antibiotic targeting the bacterial ribosome
10.1038/s41586-025-08723-7 · 2025 · External reference
A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome
10.1038/s41586-026-10589-2 · 2026 · External reference
Therapeutic potential and resistance of proline-rich antimicrobial peptides
10.1016/j.cbpa.2026.102699 · 2026 · External reference
Potent anti-candida fraction isolated from Capsicum chinense fruits contains an antimicrobial peptide that is similar to plant defensin and is able to inhibit the activity of different α-amylase enzymes
10.1007/s12602-020-09739-3 · 2021 · External reference
Adevonin, a novel synthetic antimicrobial peptide designed from the Adenanthera pavonina trypsin inhibitor (ApTI) sequence
10.1080/20477724.2018.1559489 · 2018 · External reference
Unveiling the function of antimicrobial peptides in relation to source and structure
10.1002/med.70016 · 2026 · External reference
Cathelicidin antimicrobial peptides mediate immune protection in marsupial neonates
10.1126/sciadv.ads6359 · 2025 · External reference
Significance of LL-37 on immunomodulation and disease outcome
2020 · External reference
Neuro-immune regulation in allergic diseases: role of neuropeptides
10.1016/j.intimp.2024.113771 · 2025 · External reference
Antimicrobial peptide delivery to lung as peptibody mRNA in anti-inflammatory lipids treats multidrug-resistant bacterial pneumonia
2025 · External reference
The contribution of human antimicrobial peptides to fungi
10.3390/ijms26062494 · 2025 · External reference
The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
10.1021/bi002656a · 2001 · External reference
Antimicrobial peptides boosted by ultrasound
10.1038/s41551-025-01388-7 · 2025 · External reference
Linking the production of reactive oxygen species to the expression of antimicrobial peptides through aquaporin in an arthropod
10.1073/pnas.2502570122 · 2025 · External reference
Antifungal potential of the novel antimicrobial peptide N1-6L7A against Penicillium digitatum in Citrus sinensis (L.) Osbeck and its mechanism of action
10.1016/j.postharvbio.2025.114022 · 2026 · External reference
Antimicrobial peptides: an update on classifications and databases
10.3390/ijms222111691 · 2021 · External reference
Fragments of cathelicidins PMAP-36 and BMAP-27 and their D-enantiomers: effects of all D substitutions on structure, protease resistance and antimicrobial properties
10.1016/j.bioorg.2025.108715 · 2025 · External reference
Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity
10.1016/j.actbio.2013.08.043 · 2014 · External reference
Development of α‑helical antimicrobial peptides with imperfect amphipathicity for superior activity and selectivity
10.1021/acs.jmedchem.4c01855 · 2024 · External reference
Molecular dynamics simulations of human antimicrobial peptide LL-37 in model POPC and POPG lipid bilayers
10.3390/ijms19041186 · 2018 · External reference
Antimicrobial peptides (AMPs): the quintessential ‘offense and defense’ molecules are more than antimicrobials
10.1016/j.biopha.2017.09.042 · 2017 · External reference
Structure of the antimicrobial peptide tachystatin A
10.1074/jbc.m111120200 · 2002 · External reference
Establishing a reference array for the CS-αβ superfamily of defensive peptides
10.1186/s13104-016-2291-0 · 2016 · External reference
Progress in the classification, optimization, activity, and application of antimicrobial peptides
10.3389/fmicb.2025.1582863 · 2025 · External reference
A fungal defensin inhibiting bacterial cell-wall biosynthesis with non-hemolysis and serum stability
10.3390/jof8020174 · 2022 · External reference
Structural analysis and activity correlation of amphiphilic cyclic antimicrobial peptides derived from the [W4R4] scaffold
10.3390/molecules28248049 · 2023 · External reference
Antimicrobial peptides and proteins: from nature’s reservoir to the laboratory and beyond
10.3389/fchem.2021.691532 · 2021 · External reference
Mechanisms of cell death induced by the neutrophil antimicrobial peptides α-defensins and LL-37
10.1007/s00011-005-0062-9 · 2006 · External reference
The human cathelicidin LL-37 — A pore-forming antibacterial peptide and host-cell modulator
10.1016/j.bbamem.2015.11.003 · 2016 · External reference
Rigidification of the Escherichia coli cytoplasm by the human antimicrobial peptide LL-37 revealed by superresolution fluorescence microscopy
10.1073/pnas.1814924116 · 2019 · External reference
FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis
10.1073/pnas.92.1.195 · 1995 · External reference
Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
10.1074/jbc.m805533200 · 2008 · External reference
The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics
10.1038/s41598-020-74401-5 · 2020 · External reference
Influence of bacterial biofilm polysaccharide structure on interactions with antimicrobial peptides: a study on Klebsiella pneumoniae
10.3390/ijms19061685 · 2018 · External reference
Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
10.1074/jbc.272.20.13088 · 1997 · External reference
Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection
10.1111/j.0022-202x.2005.23713.x · 2005 · External reference
Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens
10.4049/jimmunol.174.8.4901 · 2005 · External reference
Derivatives of the mouse cathelicidin-related antimicrobial peptide (CRAMP) inhibit fungal and bacterial biofilm formation
10.1128/aac.03045-14 · 2014 · External reference
Antimicrobial peptide CRAMP (16–33) stalls bacterial cytokinesis by inhibiting FtsZ assembly
10.1021/bi501115p · 2014 · External reference
Cathelicidin antimicrobial peptide expression in neutrophils and neurons antagonistically modulates neuroinflammation
2024 · External reference
Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
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