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antimicrobial peptide

Magainin

Published evidence · coverage incomplete
Anatomical contextAnatomy connections are not mapped yet.

No body region is highlighted until this profile has a supported anatomical connection. This does not mean the peptide has no biological effects.

Read published mechanism findings ↓

At a glance

What is it—and why does it matter?

Magainin 2 is described as an α-helical peptide, meaning it adopts an alpha-helix secondary structure under relevant conditions. On the negatively charged DPPG monolayer, magainin 2 adopts an α-helical structure with deep insertion and a surface-parallel orientation, indicating a defined interfacial conformation. In the antimicrobial-peptide literature described here, the emphasis is on antibacterial research; Magainin II and its derivative Pexiganan (MSI-78) are cited as examples of this focus.

Sources for this introduction: [1] [2] [3]

This published profile is a reference in progress. Findings retain their source context; missing topics are marked below.

What is it?

A molecule, not a product name.

Identity

StAMP51.2 is described as a stapled magainin 2 peptide (a conformationally constrained derivative of magainin 2).

Sources[2]pubmedCancer Susceptibility to Stapled Oncolytic Peptides Is Dictated by Membrane Cholesterol and Inflammatory Signaling.StAMP51.2, a stapled magainin 2 peptide
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “StAMP51.2, a stapled magainin 2 peptide”

    Cancer Susceptibility to Stapled Oncolytic Peptides Is Dictated by Membrane Cholesterol and Inflammatory Signaling. · UNLABELLED

    pubmed:41784645:0f6d25891a7b:0f6d25891a7b

Identity

Magainin 2 is classified as a natural antimicrobial peptide (AMP) and was one of the membrane-active peptides examined for effects on lipid-bilayer dynamics.

Sources[6]pubmedBilayer Permeabilization and the 'Sand-in-a-Gearbox' Mechanism for Membrane-Active Molecules: Which Is Which?We systematically investigated how membrane dynamics is affected by a set of well-characterized yet highly diverse peptides: the natural AMP magainin 2, the toxin melittin, the synthetic peptides LAH4 and Killer-FLIP, and small membrane-active peptidomimetics with bactericidal activity.
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “We systematically investigated how membrane dynamics is affected by a set of well-characterized yet highly diverse peptides: the natural AMP magainin 2, the toxin melittin, the synthetic peptides LAH4 and Killer-FLIP, and small membrane-active peptidomimetics with bactericidal activity.”

    Bilayer Permeabilization and the 'Sand-in-a-Gearbox' Mechanism for Membrane-Active Molecules: Which Is Which? · Abstract

    pubmed:42650666:419a39a0b6b5:419a39a0b6b5

Identity

Magainin 2 is described as an α-helical peptide, meaning it adopts an alpha-helix secondary structure under relevant conditions.

Sources[1]pubmedAlkyl-tuned hydrophobic assistance boosts hydrogen bond-directed solvation regulation of α-helix magainin in choline carboxylate ionic liquids.the α-helical peptide Magainin 2 (Mag2)[4]pubmedAromatic Fluorination Enhances the Hydrophobicity and Antimicrobial Activity of Magainin 2.Inspired by the structure of the natural antimicrobial peptide magainin 2 (MG),
Source records
2
Independent studies
2

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “the α-helical peptide Magainin 2 (Mag2)”

    Alkyl-tuned hydrophobic assistance boosts hydrogen bond-directed solvation regulation of α-helix magainin in choline carboxylate ionic liquids. · Abstract

    pubmed:41110235:9cd11a190159:9cd11a190159
  2. supports · Source-backed record
    “Inspired by the structure of the natural antimicrobial peptide magainin 2 (MG),”

    Aromatic Fluorination Enhances the Hydrophobicity and Antimicrobial Activity of Magainin 2. · Abstract

    pubmed:42587486:fecf732717d3:fecf732717d3

How does it work?

Target, response, and disposition.

Mechanism

In the DPPG monolayer, magainin 2 is organized such that hydrophobic side chains are oriented toward the acyl chains while cationic residues engage the polar headgroup region, consistent with charge-driven interfacial positioning.

Sources[3]pubmedCharge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity.with hydrophobic residues facing the lipid chains and cationic residues interacting with the polar headgroups.
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “with hydrophobic residues facing the lipid chains and cationic residues interacting with the polar headgroups.”

    Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. · Abstract

    pubmed:42501887:11b64ada3afe:11b64ada3afe

Mechanism

Specular neutron reflectometry was used to probe how the cationic antimicrobial peptide magainin 2 associates with and inserts into lipid monolayers designed to mimic bacterial versus mammalian membranes.

Sources[3]pubmedCharge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity.Here, we investigate the interfacial organisation and membrane insertion of the cationic antimicrobial peptide magainin 2 using specular neutron reflectometry on lipid monolayers that mimic bacterial and mammalian membranes.
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “Here, we investigate the interfacial organisation and membrane insertion of the cationic antimicrobial peptide magainin 2 using specular neutron reflectometry on lipid monolayers that mimic bacterial and mammalian membranes.”

    Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. · Abstract

    pubmed:42501887:11b64ada3afe:11b64ada3afe

Mechanism

StAMP51.2 is reported to have been optimized for selective membrane lysis of Gram-negative bacteria, indicating a membrane-disruptive mechanism in that setting.

Sources[2]pubmedCancer Susceptibility to Stapled Oncolytic Peptides Is Dictated by Membrane Cholesterol and Inflammatory Signaling.previously optimized for selective membrane lysis of Gram-negative bacteria
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “previously optimized for selective membrane lysis of Gram-negative bacteria”

    Cancer Susceptibility to Stapled Oncolytic Peptides Is Dictated by Membrane Cholesterol and Inflammatory Signaling. · UNLABELLED

    pubmed:41784645:0f6d25891a7b:0f6d25891a7b

Mechanism

The work operationalized membrane-type differences by using negatively charged dipalmitoylphosphatidylglycerol (DPPG) and zwitterionic dipalmitoylphosphatidylcholine (DPPC) monolayers as respective bacterial- and mammalian-mimetic interfaces for magainin 2.

Sources[3]pubmedCharge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity.Negatively charged dipalmitoylphosphatidylglycerol (DPPG) and zwitterionic dipalmitoylphosphatidylcholine (DPPC) were used as respective representative model systems.
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “Negatively charged dipalmitoylphosphatidylglycerol (DPPG) and zwitterionic dipalmitoylphosphatidylcholine (DPPC) were used as respective representative model systems.”

    Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. · Abstract

    pubmed:42501887:11b64ada3afe:11b64ada3afe

Mechanism

In the zwitterionic DPPC monolayer, magainin 2 exhibits weak/limited association and a broad (diffuse) interfacial distribution spanning headgroup and acyl-chain regions, consistent with a predominantly disordered structural state.

Sources[3]pubmedCharge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity.In contrast, at the DPPC interface, the peptide displays limited interaction with the monolayer and a diffuse intensity distribution across the headgroup and acyl-chain regions, consistent with a largely disordered conformation.
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “In contrast, at the DPPC interface, the peptide displays limited interaction with the monolayer and a diffuse intensity distribution across the headgroup and acyl-chain regions, consistent with a largely disordered conformation.”

    Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. · Abstract

    pubmed:42501887:11b64ada3afe:11b64ada3afe

Mechanism

On the negatively charged DPPG monolayer, magainin 2 adopts an α-helical structure with deep insertion and a surface-parallel orientation, indicating a defined interfacial conformation.

Sources[3]pubmedCharge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity.At the DPPG interface, the magainin 2 α-helix inserts deeply and adopts an orientation parallel to the membrane surface
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “At the DPPG interface, the magainin 2 α-helix inserts deeply and adopts an orientation parallel to the membrane surface”

    Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. · Abstract

    pubmed:42501887:11b64ada3afe:11b64ada3afe

What has been studied?

What the evidence says.

Comparative evidence

In the antimicrobial-peptide literature described here, the emphasis is on antibacterial research; Magainin II and its derivative Pexiganan (MSI-78) are cited as examples of this focus.

Sources[5]pubmedUnveiling the Potential of Magainin Derivatives against Candida Species.Antimicrobial peptides are promising alternative antimicrobial agents, but most work focuses on antibacterial studies, including Magainin II and its derivative Pexiganan (MSI-78).
Source records
1
Independent studies
1

Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.

Exact passages, locators, and provenance
  1. supports · Source-backed record
    “Antimicrobial peptides are promising alternative antimicrobial agents, but most work focuses on antibacterial studies, including Magainin II and its derivative Pexiganan (MSI-78).”

    Unveiling the Potential of Magainin Derivatives against Candida Species. · Abstract

    pubmed:42593921:41e70dd79a5b:41e70dd79a5b

Risks and interactions

Risks, organized for scanning.

This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.

Products and regulatory status

Same ingredient. Different records.

This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.

Administration context

The practical clinical context.

This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.

Research status + gaps

What still needs better answers?

  • No publishable claim yet for: administration, contraindication, effect, interaction, regulatory, safety
  • 33 compiled claim(s) withheld by automated assurance: assurance_score_below_0.58 (32), assurance_score_below_0.72 (1), current_regulatory_source_required (1), extraction_ambiguity (33), high_risk_requires_regulatory_or_two_independent_sources (1), no_direct_support (33)

These are the limits of this profile, not an exhaustive list of scientific uncertainties.

References + discovery

Open the records yourself.

  1. Alkyl-tuned hydrophobic assistance boosts hydrogen bond-directed solvation regulation of α-helix magainin in choline carboxylate ionic liquids. ↗

    pubmed · published 2026-02-01 · retrieved 2026-08-27T11:48:55Z

  2. Cancer Susceptibility to Stapled Oncolytic Peptides Is Dictated by Membrane Cholesterol and Inflammatory Signaling. ↗

    pubmed · published 2026-06-01 · retrieved 2026-08-27T11:48:55Z

  3. Charge-dependent insertion of the antimicrobial peptide magainin 2 into lipid monolayers probed by neutron reflectivity. ↗

    pubmed · published 2026-10-01 · retrieved 2026-08-27T11:48:55Z

  4. Aromatic Fluorination Enhances the Hydrophobicity and Antimicrobial Activity of Magainin 2. ↗

    pubmed · published 2026-08-12 · retrieved 2026-08-27T11:48:55Z

  5. Unveiling the Potential of Magainin Derivatives against Candida Species. ↗

    pubmed · published 2026-08-13 · retrieved 2026-08-27T11:48:55Z

  6. Bilayer Permeabilization and the 'Sand-in-a-Gearbox' Mechanism for Membrane-Active Molecules: Which Is Which? ↗

    pubmed · published 2026-07-31 · retrieved 2026-08-27T11:48:55Z

Publication history and provenance

Version 2 · Automated assessment · 2026-08-27T11:48:55Z

d50b8e786d2a72f5a865fafe6d65a0658deaee2bedbb69953e4576ee66565889