[Ala8,13,18]-Magainin II amide (CAS 117665-48-2)

[Ala8,13,18]-Magainin II amide is an analog of Magainin II, a well-known antimicrobial peptide originally isolated from the skin of the African clawed frog, Xenopus laevis. This synthetic peptide is modified by substituting alanine at positions 8, 13, and 18, which enhances its stability and activity. The primary mechanism of action of [Ala8,13,18]-Magainin II amide involves disrupting bacterial cell membranes. It binds to the phospholipid bilayer, integrates into the membrane, and forms pores, leading to increased membrane permeability, leakage of cellular contents, and ultimately cell death. In research, [Ala8,13,18]-Magainin II amide is extensively used to study the structure-activity relationships of antimicrobial peptides and their interactions with microbial membranes. This peptide serves as a model for understanding how specific amino acid substitutions affect the peptide′s ability to interact with and disrupt membranes. Researchers utilize this compound to explore the mechanisms underlying membrane selectivity and specificity, providing insights into the design of peptides with enhanced antimicrobial properties. Additionally, [Ala8,13,18]-Magainin II amide is employed in biophysical studies to investigate the dynamics of peptide-membrane interactions using techniques such as circular dichroism spectroscopy, fluorescence microscopy, and electron microscopy. The research applications of [Ala8,13,18]-Magainin II amide contribute significantly to the fields of microbiology, biophysics, and peptide chemistry, advancing our understanding of antimicrobial mechanisms.