Antimicrobial Peptides: Natural Defense Molecules

Every surface of the human body that contacts the outside world — skin, lungs, gut, urinary tract — is guarded by a chemical defense system older than the adaptive immune system itself. Antimicrobial peptides (AMPs) are a foundational part of that defense: small proteins, typically 10 to 50 amino acids, that kill bacteria, fungi, and viruses through mechanisms fundamentally different from conventional antibiotics.

That last point matters. Antibiotic resistance is projected to directly cause 39 million deaths over the next 25 years, with another 169 million deaths from indirect causes (Lancet, 2024). Conventional antibiotics hit specific molecular targets — an enzyme, a ribosome, a metabolic pathway — and bacteria can develop resistance by mutating that single target. AMPs take a broader approach, targeting the bacterial membrane itself. Mutating away from that vulnerability would require bacteria to fundamentally reorganize their cell membrane architecture — possible in theory, but far more difficult in practice.

As of January 2025, the APD3 database catalogs 5,099 antimicrobial peptides, including 3,306 natural AMPs from six kingdoms of life, along with 1,299 synthetic and 231 computationally designed variants (APD3, 2025). This guide covers how they work, which families matter most, and where clinical development stands.

How Antimicrobial Peptides Work
Membrane Disruption: The Three Models
Beyond the Membrane: Intracellular and Immunomodulatory Actions
Defensins: The Largest Human AMP Family
Cathelicidins: LL-37 and Its Derivatives
Magainins and Amphibian Peptides
Other AMP Families of Note
Why Resistance Is Harder to Develop
AMPs and Antibiotic Resistance: The Clinical Case
Clinical Development: Approved Drugs and Pipeline
Challenges in AMP Drug Development
FAQ
The Bottom Line
References

How Antimicrobial Peptides Work {#how-antimicrobial-peptides-work}

The antimicrobial activity of AMPs rests on a simple physical principle: most AMPs are cationic (positively charged) and amphipathic (having both hydrophobic and hydrophilic faces). Bacterial membranes are rich in negatively charged phospholipids — phosphatidylglycerol, cardiolipin, and lipopolysaccharides in Gram-negative species. Mammalian cell membranes, by contrast, have their negative charges mostly on the inner leaflet and present neutral phosphatidylcholine on the outer surface.

This charge difference is what gives AMPs their selectivity. The positively charged peptide is electrostatically attracted to the negatively charged bacterial surface and relatively indifferent to the neutral mammalian membrane. It is not perfect selectivity — at high enough concentrations, many AMPs will damage host cells — but it provides a therapeutic window.

Once an AMP reaches the bacterial surface, what happens next depends on the specific peptide. The mechanisms fall into two broad categories: membrane-targeting and intracellular-targeting actions. Most AMPs use membrane disruption as their primary killing mechanism, though many also have intracellular effects that contribute to bacterial death (Lei et al., 2019).

Membrane Disruption: The Three Models {#membrane-disruption-the-three-models}

Researchers have proposed three classical models to explain how AMPs destroy bacterial membranes. The reality is likely more complex than any single model suggests — many peptides may use elements of multiple mechanisms — but these frameworks remain the standard way to discuss AMP action (Wimley, 2010).

The Barrel-Stave Model

In this model, AMP molecules insert perpendicularly into the lipid bilayer and arrange themselves in a ring — like staves of a barrel — around a central aqueous pore. The hydrophobic faces of the peptides contact the lipid tails, while the hydrophilic faces line the pore interior. Cellular contents leak through these pores, leading to osmotic imbalance and cell death.

The barrel-stave model requires peptides that are long enough to span the membrane and hydrophobic enough to integrate stably into the lipid core. Alamethicin, a 20-amino-acid fungal peptide, is the best-characterized example — and notably, it may be the only peptide for which this mechanism has been definitively confirmed. The tight peptide-peptide packing required for barrel-stave pores is only feasible for very weakly charged peptides; otherwise electrostatic repulsion between the charged peptides destabilizes the structure.

The Toroidal Pore Model

The toroidal pore model is more common. Here, AMPs insert into the membrane and cause the lipid molecules themselves to bend inward, creating a pore lined by both peptides and lipid headgroups. The key difference from barrel-stave: in toroidal pores, the lipid bilayer curves continuously through the pore, so the inner surface is a mixture of peptide and lipid rather than peptide alone.

Toroidal pore formation often requires a threshold concentration — peptides accumulate on the membrane surface until reaching a critical ratio (typically around 1 peptide per 20-100 lipids), at which point pores form cooperatively. Magainin 2, melittin, and LL-37 are thought to act through this mechanism.

The Carpet Model

The carpet model describes peptides that do not form discrete pores at all. Instead, AMPs coat the membrane surface like a carpet, lying parallel to the bilayer. When the local peptide concentration reaches a sufficient level, the accumulated peptides disrupt the membrane integrity in a detergent-like fashion — essentially dissolving patches of the membrane. At very high concentrations, carpet-model peptides essentially solubilize the membrane into peptide-lipid micelles.

This mechanism does not require specific peptide-peptide interactions or membrane insertion. It is the most general model and may apply to many natural AMPs, particularly short or highly charged peptides that cannot span the full bilayer.

The Practical Reality

These three models describe the end state of membrane disruption, not necessarily the pathway that leads there. Real peptide-membrane interactions likely involve a sequence of events — initial electrostatic attraction, surface accumulation, partial insertion, and then one or more of these disruption modes depending on the peptide's properties and the membrane composition. A 2023 review in Biophysical Reviews emphasized that most AMPs probably do not follow a single model exclusively but rather exhibit behaviors on a spectrum between these idealized descriptions (PMC, 2023).

Beyond the Membrane: Intracellular and Immunomodulatory Actions {#beyond-the-membrane}

Membrane disruption is not the whole story. Many AMPs have intracellular targets that contribute to — or in some cases are primarily responsible for — their antimicrobial activity.

Intracellular targets identified in various AMPs include:

DNA and RNA synthesis (binding nucleic acids and inhibiting replication)
Protein synthesis (interfering with ribosomal function)
Cell wall synthesis (disrupting peptidoglycan assembly)
Cell division (inhibiting septum formation)
Protease activity (degrading bacterial enzymes)

Immunomodulation is increasingly recognized as a critical function of AMPs in vivo. Rather than simply killing bacteria directly, many AMPs orchestrate the immune response by:

Recruiting immune cells (neutrophils, monocytes, dendritic cells) to infection sites
Modulating cytokine production (interleukins, TNF-alpha, interferons)
Promoting wound healing and tissue repair
Neutralizing bacterial endotoxins (lipopolysaccharides)

This dual function — direct antimicrobial action plus immune modulation — may explain why AMPs remain effective in vivo at concentrations below their minimum inhibitory concentration (MIC) measured in laboratory assays. The peptide does not need to kill every bacterium directly; it needs to tip the balance in favor of the immune system.

Antiviral activity has also been documented for many AMPs. Some peptides directly disrupt viral envelopes (similar to their action on bacterial membranes), while others block viral entry into host cells or stimulate antiviral immune pathways. Vitamin D-induced production of cathelicidins and defensins is one mechanism linking vitamin D status to antiviral defense.

Defensins: The Largest Human AMP Family {#defensins}

Defensins are small (29-45 amino acids), cysteine-rich peptides that form the body's most abundant antimicrobial peptide family. They are characterized by three conserved disulfide bonds that create a compact, stable beta-sheet structure resistant to proteolytic degradation.

Alpha-Defensins

Humans produce six alpha-defensins. Four of them — HNP-1 through HNP-4 (human neutrophil peptides) — are stored in neutrophil granules and released during phagocytosis. Neutrophils contain massive quantities: HNP-1 through HNP-3 together make up about 5-7% of total neutrophil protein. HNP-1 is the most abundant antimicrobial peptide in human neutrophils.

The other two alpha-defensins, HD-5 and HD-6, are produced by Paneth cells in the small intestine. They provide a frontline defense against intestinal pathogens and play a role in shaping the gut microbiome. HD-5 is effective against both bacteria and some viruses, while HD-6 has a unique mechanism — it self-assembles into "nanonets" that trap bacteria rather than killing them directly.

Beta-Defensins

Beta-defensins are produced primarily by epithelial cells across mucosal surfaces — skin, airways, urogenital tract, and GI tract. Over 30 human beta-defensin genes have been identified, though only a few are well characterized:

HBD-1 (human beta-defensin 1) is constitutively expressed in the kidneys, respiratory tract, and urogenital tract. Unlike most other defensins, its production is not strongly upregulated by infection — it provides a constant baseline defense.

HBD-2 is induced by bacterial infection, inflammation, and pro-inflammatory cytokines. It is active against Gram-negative bacteria and yeasts and was the first inducible human beta-defensin discovered.

HBD-3 has the broadest antimicrobial spectrum of the beta-defensins, with potent activity against both Gram-positive and Gram-negative bacteria, including methicillin-resistant Staphylococcus aureus (MRSA). Skin keratinocytes produce HBD-3 to reinforce the epithelial barrier during infection.

Therapeutic Challenges with Defensins

Despite their obvious biological importance, therapeutic development of defensins has been difficult. Their disulfide bonds make them expensive to synthesize. Their activity is salt-sensitive — defensin antimicrobial potency drops significantly at the salt concentrations found in many body fluids. And manipulating defensin expression raises the theoretical risk of disrupting the normal microbiome composition, an unintended consequence that is hard to predict or monitor.

Cathelicidins: LL-37 and Its Derivatives {#cathelicidins}

While other mammals produce multiple cathelicidins, humans make just one: LL-37, a 37-amino-acid alpha-helical peptide named for its two N-terminal leucine residues. It is stored as an inactive precursor (hCAP-18) in neutrophil granules and epithelial cells, then activated by protease cleavage when released.

Where LL-37 Is Found

LL-37 is produced in neutrophils, monocytes, mast cells, natural killer cells, and epithelial cells of the skin, airways, GI tract, and urogenital tract. It is present in wound fluid, sweat, airway surface liquid, breast milk, and seminal plasma. This broad distribution underlines its role as a general-purpose defense molecule.

What LL-37 Does

LL-37 has antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and enveloped viruses. It works primarily through the toroidal pore model of membrane disruption, though its immunomodulatory functions may be equally important in vivo.

As an immune modulator, LL-37 recruits immune cells to infection sites, stimulates wound healing, promotes angiogenesis (new blood vessel formation), and can suppress biofilm formation by several bacterial species. It also has anti-inflammatory properties at certain concentrations, helping to prevent excessive immune responses that can damage host tissue.

LL-37 in Disease

Dysregulation of LL-37 production is associated with several diseases. Rosacea involves overexpression and abnormal processing of LL-37 in facial skin. Crohn's disease features reduced colonic LL-37 expression, potentially contributing to bacterial invasion. Psoriasis involves LL-37-mediated activation of dendritic cells against self-DNA, driving autoimmune inflammation.

Therapeutic Development

LL-37 itself faces practical barriers as a drug — proteolytic instability, potential cytotoxicity at high doses, and high production costs. Research has focused on shorter, more stable derivatives. An LL-37-derived peptide completed a Phase I/II clinical trial in 2024 for melanoma, demonstrating antitumor effects — an application beyond traditional antimicrobial use.

A 2025 review in the International Journal of Molecular Sciences compiled recent advances in LL-37 modifications, including D-amino acid substitutions, sequence truncations, and cyclization approaches aimed at improving stability and reducing toxicity while maintaining antimicrobial activity (IJMS, 2025).

Magainins and Amphibian Peptides {#magainins-and-amphibian-peptides}

Frog skin has been a remarkably productive source of AMPs. Michael Zasloff's 1987 discovery of magainins in the African clawed frog (Xenopus laevis) was a landmark moment — he noticed that surgical wounds on the frogs healed without infection despite non-sterile conditions, leading him to isolate the peptides responsible.

Magainin 1 and 2 are 23-amino-acid alpha-helical peptides that form toroidal pores in bacterial membranes. Magainin 2 became the template for pexiganan (MSI-78), a synthetic 22-amino-acid analog that entered clinical trials for diabetic foot ulcer infections. Though pexiganan was shown to be safe for topical use, it failed to demonstrate superiority over standard care in Phase III trials and was denied FDA approval.

Amphibian skin has since yielded hundreds of additional AMPs, including dermaseptins, temporins, bombinins, and esculentins. While none have reached clinical approval, they continue to serve as templates for synthetic AMP design.

Other AMP Families of Note {#other-amp-families}

Polymyxins (polymyxin B and colistin/polymyxin E) are among the oldest clinically used AMPs, first discovered in the 1940s. They are cyclic lipopeptides produced by Bacillus polymyxa that bind lipopolysaccharides in Gram-negative bacterial outer membranes. Colistin is often a "last resort" antibiotic for multidrug-resistant Gram-negative infections, though its use is limited by nephrotoxicity.

Daptomycin (Cubicin) is a cyclic lipopeptide antibiotic approved in 2003 for Gram-positive infections, including MRSA. It forms a complex with phosphatidylglycerol and lipid II in bacterial membranes, causing rapid depolarization and cell death. Daptomycin is the most commercially successful FDA-approved membrane-active AMP and is the clinical benchmark for the field.

Gramicidin and tyrothricin are among the earliest AMP-based drugs. Gramicidin S, a cyclic decapeptide, forms ion channels in bacterial membranes. These peptides are used in topical preparations (throat lozenges, eye drops) because their toxicity precludes systemic use.

Nisin is a 34-amino-acid lantibiotic (lanthionine-containing antibiotic) produced by Lactococcus lactis. It has been used safely in the food industry as a preservative for over 50 years — one of the longest track records of any AMP in practical use. Nisin kills bacteria by binding to lipid II (a peptidoglycan precursor) and forming pores, combining two killing mechanisms in a single molecule.

Why Resistance Is Harder to Develop {#why-resistance-is-harder}

The central promise of AMPs as therapeutic agents is that they make resistance development harder. The reasoning is straightforward.

Conventional antibiotics hit specific molecular targets. Penicillin inhibits a specific transpeptidase enzyme. Ciprofloxacin targets DNA gyrase. Erythromycin binds a specific ribosomal subunit. Bacteria can develop resistance by mutating these specific targets, producing enzymes that degrade the drug, pumping the drug out, or modifying the target so the drug no longer binds. A single gene mutation can be enough.

AMPs target the bacterial membrane — a structure made of hundreds of different lipid and protein components. Changing membrane composition enough to resist AMP attack would require coordinated changes across many genes, potentially compromising membrane function in the process. Moreover, AMPs often act through multiple mechanisms simultaneously (membrane disruption plus intracellular targeting), meaning bacteria would need to develop resistance to several killing pathways at once.

This does not mean resistance is impossible. Bacteria have evolved several strategies to reduce AMP susceptibility:

Modifying membrane lipid composition to reduce negative charge
Producing surface molecules that trap or repel AMPs
Expressing efflux pumps that remove AMPs from the membrane
Secreting proteases that degrade AMPs before they reach the cell

However, these resistance mechanisms typically provide only partial protection (raising the MIC by 2-8 fold rather than creating complete resistance) and often carry fitness costs that make them unstable in the absence of continued AMP exposure. Full resistance to membrane-targeting AMPs — comparable to the complete resistance bacteria develop against some conventional antibiotics — has not been widely observed.

AMPs and Antibiotic Resistance: The Clinical Case {#amps-and-antibiotic-resistance}

The World Health Organization lists antimicrobial resistance as one of the top 10 global health threats. Antibiotic-resistant infections are estimated to contribute to 4.95 million deaths annually, and projections suggest this number will continue rising without new therapeutic strategies.

AMPs fit into the antibiotic resistance picture in several ways:

As direct replacements. For infections caused by multidrug-resistant organisms, AMPs with different mechanisms of action could provide treatment options where conventional antibiotics fail. Daptomycin already fills this role for MRSA infections.

As combination partners. AMPs that disrupt bacterial membranes can increase the permeability of bacteria to conventional antibiotics, creating synergistic effects. A sub-lethal dose of an AMP, combined with a conventional antibiotic, can be more effective than either agent alone — and the combination may slow resistance development to both agents.

As biofilm disruptors. Bacterial biofilms — structured communities encased in a protective matrix — are notoriously resistant to conventional antibiotics. Many AMPs can penetrate biofilms and disrupt their structure, potentially making the enclosed bacteria vulnerable to other treatments.

As immune system enhancers. By boosting the innate immune response, AMPs may help clear infections without applying the same selective pressure as direct-acting antibiotics, potentially reducing the driving force for resistance evolution.

A 2025 review in Annals of Medicine and Surgery concluded that AMPs represent "a promising frontier to combat antibiotic-resistant pathogens," while emphasizing that their clinical translation requires addressing production costs, stability issues, and the need for better delivery systems (AMS, 2025).

Clinical Development: Approved Drugs and Pipeline {#clinical-development}

Despite the biological promise, the clinical development of AMPs has been slower and more difficult than early enthusiasm suggested. Over the past 40 years, fewer than 50 AMPs have entered clinical trials. Only about 12 have received FDA or EMA approval, and most of those approvals happened over a decade ago (JTM, 2025).

FDA-Approved AMP-Based Drugs

Drug	Type	Year	Indication
Polymyxin B	Cyclic lipopeptide	1964	Gram-negative infections
Colistin (Polymyxin E)	Cyclic lipopeptide	1959	Gram-negative infections (last resort)
Bacitracin	Cyclic peptide	1948	Topical infections
Gramicidin	Linear peptide	1940s	Topical infections
Daptomycin	Cyclic lipopeptide	2003	MRSA and Gram-positive infections
Tyrothricin	Peptide mixture	1940s	Topical infections

Several of these are cyclic peptides — a structural feature that confers greater protease resistance and is increasingly recognized as clinically relevant for AMP drug design.

Key Pipeline Candidates

Murepavadin (POL7080) is a 14-amino-acid cyclic peptide targeting the outer membrane protein LptD of Pseudomonas aeruginosa. It showed potent activity against extensively drug-resistant strains, including colistin-resistant isolates. However, its intravenous Phase III trial for hospital-acquired pneumonia was halted due to unexpectedly high rates of acute kidney injury (56% in the treatment group versus 25-40% in controls). Development has pivoted to inhaled formulations, which may avoid systemic toxicity.

Brilacidin (PMX-30063) is a synthetic defensin-mimetic that completed Phase II trials for acute bacterial skin infections. Its non-peptide structure (it is a small molecule that mimics defensin's membrane-disrupting properties) may give it better pharmacokinetic properties than natural peptide AMPs.

PL-5 Spray is a topical AMP spray that completed Phase II trials for wound infections in China, demonstrating safety and efficacy with low potential to induce resistance.

Omiganan (an indolicidin analog) and iseganan (a protegrin analog) have had mixed results in clinical trials for skin infections and oral mucositis, respectively. Both demonstrated safety but struggled to show superiority over existing treatments.

An LL-37-derived peptide completed Phase I/II trials for melanoma in 2024, representing an expansion of AMPs beyond purely antimicrobial applications into immunotherapy.

Challenges in AMP Drug Development {#challenges-in-amp-drug-development}

The gap between biological potential and clinical success reflects several practical obstacles.

Production cost. Solid-phase peptide synthesis for AMPs is expensive compared to conventional antibiotic manufacturing. A typical AMP of 20-40 amino acids costs significantly more to produce than a small-molecule antibiotic, especially at the scale needed for systemic therapy. Recombinant production and fermentation approaches are being developed but are not yet cost-competitive for most candidates.

Stability. Natural AMPs are rapidly degraded by proteases in blood and tissues, giving them short half-lives that limit systemic use. Topical applications avoid this problem (which is why most clinically advanced AMPs are topical formulations), but systemic delivery requires modifications — D-amino acid substitution, cyclization, non-natural amino acid incorporation, PEGylation, or encapsulation in nanoparticles.

Toxicity. The same membrane-disrupting activity that kills bacteria can damage host cells at higher concentrations. The therapeutic window — the gap between effective antimicrobial concentration and toxic concentration — is narrower for many AMPs than for conventional antibiotics. Murepavadin's nephrotoxicity in Phase III trials illustrates this challenge.

Efficacy hurdles. Several AMP candidates (pexiganan, iseganan) failed clinical trials not because they were toxic but because they could not demonstrate superiority over existing treatments. The regulatory bar for new anti-infectives is high, and AMPs must compete with decades of optimized conventional antibiotics.

Spectrum management. AMPs' broad-spectrum activity is a double-edged sword. While it is useful against resistant organisms, it also means AMPs can disrupt the normal microbiome — the same concern that limits broad-spectrum antibiotic use.

The Path Forward

A 2025 review in Frontiers in Cellular and Infection Microbiology outlined the most promising approaches for overcoming these challenges (FCIMB, 2025):

Structural engineering: Non-natural amino acids, cyclization, and peptidomimetic scaffolds improve stability and selectivity
Advanced delivery systems: Nanoparticle encapsulation, hydrogel formulations, and conjugation with targeting moieties improve tissue specificity and reduce systemic toxicity
AI-driven design: Machine learning models trained on known AMP sequences and activities can generate novel candidates optimized for specific properties — potency, selectivity, stability, or cost of synthesis
Combination strategies: Pairing AMPs with conventional antibiotics at sub-inhibitory concentrations may achieve clinical efficacy while keeping costs down

FAQ {#faq}

What is the difference between antimicrobial peptides and antibiotics?

AMPs are peptides (short proteins) that primarily kill bacteria by disrupting their cell membranes, while conventional antibiotics are mostly small molecules that inhibit specific bacterial enzymes or metabolic processes. AMPs are part of the innate immune system and have been around for hundreds of millions of years of evolution. Antibiotics are typically discovered from or inspired by microbial natural products. The key practical difference: bacteria find it harder to develop resistance to membrane-targeting AMPs than to target-specific antibiotics.

Are defensins and cathelicidins found in humans?

Yes. Humans produce six alpha-defensins, over 30 beta-defensins, and one cathelicidin (LL-37). Defensins are concentrated in neutrophils and epithelial surfaces. LL-37 is produced by neutrophils, monocytes, and epithelial cells throughout the body. Together, these peptides form a chemical barrier at every surface exposed to potential pathogens.

Can bacteria become resistant to antimicrobial peptides?

Bacteria can develop partial resistance — reducing their susceptibility by modifying membrane composition, expressing efflux pumps, or secreting AMP-degrading proteases. However, complete resistance comparable to what develops against conventional antibiotics has not been widely observed. The multi-target nature of AMP action (membrane disruption plus intracellular effects plus immune modulation) makes resistance development slow and costly for bacteria.

Why are there so few FDA-approved AMP drugs?

Several factors: high production costs, poor pharmacokinetic properties (short half-lives, limited oral bioavailability), narrow therapeutic windows between antimicrobial and toxic concentrations, and clinical trial designs that struggled to demonstrate superiority over existing treatments. Most approved AMP drugs are used topically or as last-resort agents for multidrug-resistant infections.

How do antimicrobial peptides relate to peptides like BPC-157 or TB-500?

They are different categories of peptides. AMPs like defensins and LL-37 kill microbes and modulate immunity. Peptides like BPC-157 and TB-500 are studied for tissue repair and regeneration. GHK-Cu bridges the gap somewhat — it is primarily studied for wound healing and anti-aging but also has some antimicrobial properties. The common thread is that all are short peptides with biological activity, but their targets and mechanisms are distinct.

What role do antimicrobial peptides play in skin health?

AMPs are the skin's first chemical defense against infection. Keratinocytes produce beta-defensins (especially HBD-2 and HBD-3) and LL-37 in response to bacteria, injury, or inflammation. These peptides kill surface pathogens, recruit immune cells, and promote wound healing. Dysregulation of skin AMP production is linked to conditions including acne, eczema, psoriasis, and rosacea.

The Bottom Line {#the-bottom-line}

Antimicrobial peptides are not a new discovery — they have been defending living organisms for hundreds of millions of years. What is new is the urgency to translate that ancient biology into modern medicine. With antibiotic resistance growing and the conventional antibiotic pipeline thinning, AMPs offer mechanisms of action that bacteria cannot easily evade.

The clinical track record so far is sobering. Fewer than 50 AMPs have reached clinical trials in four decades, and several prominent candidates have failed at late stages. The challenges — cost, stability, toxicity, and the high bar for clinical proof — are real.

But the field is not standing still. Computational design is generating novel AMP candidates at unprecedented speed. Structural engineering is solving the stability and selectivity problems that plagued earlier generations. Nanoparticle delivery systems are expanding the routes and targets available. And the success of daptomycin — a cyclic lipopeptide AMP that generates over a billion dollars in annual revenue — proves that AMP-based drugs can work commercially.

For more on specific antimicrobial peptides, see our guides on LL-37 and defensins. For related topics in peptide science, our guides on peptide mechanisms of action and peptide synthesis methods provide useful background.

References {#references}

Lei, J., et al. (2019). The antimicrobial peptides and their potential clinical applications. American Journal of Translational Research, 11(7), 3919-3931. PMC
Wimley, W.C. (2010). Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chemical Biology, 5(10), 905-917. PMC
Mookherjee, N., et al. (2020). Antimicrobial host defence peptides: functions and clinical potential. Nature Reviews Drug Discovery, 19(5), 311-332. PubMed
Huan, Y., et al. (2020). Antimicrobial peptides: Classification, design, application and research progress in multiple fields. Frontiers in Microbiology, 11, 582779. PMC
Chen, Y., et al. (2025). Antimicrobial peptide biological activity, delivery systems and clinical translation status and challenges. Journal of Translational Medicine, 23, 234. PMC
Solanki, D., et al. (2025). Antimicrobial peptides: A promising frontier to combat antibiotic-resistant pathogens. Annals of Medicine and Surgery. LWW
Baturin, A., et al. (2025). Unlocking the power of antimicrobial peptides: Advances in production, optimization, and therapeutics. Frontiers in Cellular and Infection Microbiology, 15, 1528583. Frontiers
Garefalaki, V., et al. (2025). Antimicrobial peptides of the cathelicidin family: Focus on LL-37 and its modifications. International Journal of Molecular Sciences, 26(16), 8103. MDPI
Dijksteel, G.S., et al. (2023). Latest developments on the mechanism of action of membrane disrupting peptides. Biophysical Reviews, 15(3), 461-473. PMC
Koehbach, J. & Craik, D.J. (2019). The vast structural diversity of antimicrobial peptides. Trends in Pharmacological Sciences, 40(7), 517-528. APD3 Database

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