$302.00 - $302.00
Magainin 1 is a 23-residue antimicrobial peptide from Xenopus laevis and one of the original members of the Magainin peptide family.
Its short linear sequence combines cationic and hydrophobic residues that support formation of an amphipathic helical structure in membrane-associated environments.
Product Information
| Property | Specification |
|---|---|
| Product Name | Magainin 1 |
| Catalog No. | AS2702 |
| CAS No. | 108433-99-4 |
| Sequence | Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser |
| One-Letter Sequence | GIGKFLHSAGKFGKAFVGEIMKS |
| Peptide Length | 23 amino acids |
| Molecular Formula | C112H177N29O28S |
| Molecular Weight | Approximately 2409.8 Da |
| C-Terminus | Free carboxyl terminus |
| Peptide Class | Linear amphipathic antimicrobial peptide |
| Purity | Crude to 98% |
Magainin 1 and Magainin 2 Sequence Differences
Magainin 1 and Magainin 2 are closely related 23-residue peptides, but they are not sequence-identical.
| Position | Magainin 1 | Magainin 2 |
|---|---|---|
| 10 | Gly | Lys |
| 22 | Lys | Asn |
These substitutions alter local charge and side-chain chemistry while preserving the overall amphipathic character of the peptide family.
We consider this pair particularly useful for sequence–function studies because researchers can examine how limited substitutions influence membrane binding and antimicrobial behavior without comparing completely unrelated peptide scaffolds.
Lipid Selectivity and Membrane Research
Magainin 1 interacts preferentially with membranes containing negatively charged lipids through a combination of electrostatic attraction and hydrophobic association.
Upon membrane binding, the peptide can acquire increased helical structure and promote leakage from anionic lipid vesicles. This makes it useful for studying how membrane charge affects peptide association and bilayer disruption.
Research Applications
Applications include antimicrobial peptide SAR, phospholipid vesicle assays, membrane leakage studies and evaluation of sequence changes affecting peptide charge or helicity.
Researchers making direct family comparisons can also review Magainin 2.
Experimental Planning
Magainin activity is sensitive to assay composition. Lipid charge, salt concentration, peptide-to-lipid ratio and the biological model can alter apparent potency or membrane leakage.
Researchers can refer to our Recommended Peptide Purity guidance when selecting material for biochemical or cell-based studies.
Frequently Asked Questions
Is Magainin 1 the same peptide as Magainin 2?
No. Both contain 23 residues, but they differ at positions 10 and 22.
What is the C-terminal form of Magainin 1?
The sequence listed here contains a free C-terminal carboxyl group rather than a C-terminal amide.
Can charge or hydrophobicity variants be prepared?
Defined substitutions and modified Magainin analogs can be evaluated through Chemical Peptide Synthesis.