Common mechanism unites membrane poration by amyloid and antimicrobial peptides | PNAS
Magainin 2-PGLa Interactions in Membranes - Two Peptides that Exhibit Synergistic Enhancement of Antimicrobial Activity | Bentham Science
The peptide design based on the essential fragment of magainin 2 (Mag2). | Download Scientific Diagram
Antiviral peptides as promising therapeutic drugs | SpringerLink
Stretch-Activated Pore of the Antimicrobial Peptide, Magainin 2 | Langmuir
Magainin 2 - Proteopedia, life in 3D
Effect of membrane potential on pore formation by the antimicrobial peptide magainin 2 in lipid bilayers - ScienceDirect
Frontiers | The Reversible Non-covalent Aggregation Into Fibers of PGLa and Magainin 2 Preserves Their Antimicrobial Activity and Synergism
Difference between Magainin-2 and Melittin Assemblies in Phosphatidylcholine Bilayers: Results from Coarse-Grained Simulations | The Journal of Physical Chemistry B
RCSB PDB - 2MAG: NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES
Highly synergistic antimicrobial activity of magainin 2 and PGLa peptides is rooted in the formation of supramolecular complexes with lipids | Scientific Reports
IJMS | Free Full-Text | Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides
Magainin 2 - an overview | ScienceDirect Topics
Interaction between Antimicrobial Peptide Magainin 2 and Nonlipid Components in the Bacterial Outer Envelope | The Journal of Physical Chemistry B