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Magainin I

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Magainin I is a peptide antibiotic with antibacterial and antiparasitic activities, originally extracted from the skin of Xenopus laevis. It has a broad spectrum of non-specific activity against a variety of microorganisms, including viruses, gram-positive and gram-negative bacteria, protozoa, yeast and fungi, and may also have hemolytic and cytotoxicity to cancer cells. Magainin 1 is a fungicide. Magainin 1 has an inhibitory effect on herpes simplex virus type 1 (HSV-1) and HSV-2.

Category

Functional Peptides

Catalog number

BAT-010525

CAS number

108433-99-4

Molecular Formula

C112H177N29O28S

Molecular Weight

2409.85

Specification
Reference Reading

IUPAC Name

(4S)-4-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[2-[[(2S,3S)-2-[(2-aminoacetyl)amino]-3-methylpentanoyl]amino]acetyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]acetyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]hexanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-5-[[(2S,3S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-1-oxohexan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid

Synonyms

H-Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser-OH; glycyl-L-isoleucyl-glycyl-L-lysyl-L-phenylalanyl-L-leucyl-L-histidyl-L-seryl-L-alanyl-glycyl-L-lysyl-L-phenylalanyl-glycyl-L-lysyl-L-alanyl-L-phenylalanyl-L-valyl-glycyl-L-alpha-glutamyl-L-isoleucyl-L-methionyl-L-lysyl-L-serine; Magainin 1 peptide, Xenopus

Appearance

White or Off-white Lyophilized Powder

Purity

>95%

Density

1.3±0.1 g/cm3

Boiling Point

2396.1±65.0°C at 760 mmHg

Sequence

GIGKFLHSAGKFGKAFVGEIMKS

Storage

Store at -20°C

Solubility

Soluble in DMSO

InChI

InChI=1S/C112H177N29O28S/c1-12-65(7)93(139-86(144)54-117)110(166)122-59-89(147)128-75(39-25-29-46-115)100(156)135-81(51-70-33-19-15-20-34-70)105(161)133-79(49-63(3)4)104(160)136-83(53-72-55-118-62-123-72)106(162)137-84(60-142)108(164)124-67(9)95(151)119-56-87(145)127-74(38-24-28-45-114)99(155)134-80(50-69-31-17-14-18-32-69)97(153)120-57-88(146)126-73(37-23-27-44-113)98(154)125-68(10)96(152)132-82(52-71-35-21-16-22-36-71)107(163)140-92(64(5)6)109(165)121-58-90(148)129-77(41-42-91(149)150)103(159)141-94(66(8)13-2)111(167)131-78(43-48-170-11)102(158)130-76(40-26-30-47-116)101(157)138-85(61-143)112(168)169/h14-22,31-36,55,62-68,73-85,92-94,142-143H,12-13,23-30,37-54,56-61,113-117H2,1-11H3,(H,118,123)(H,119,151)(H,120,153)(H,121,165)(H,122,166)(H,124,164)(H,125,154)(H,126,146)(H,127,145)(H,128,147)(H,129,148)(H,130,158)(H,131,167)(H,132,152)(H,133,161)(H,134,155)(H,135,156)(H,136,160)(H,137,162)(H,138,157)(H,139,144)(H,140,163)(H,141,159)(H,149,150)(H,168,169)/t65-,66-,67-,68-,73-,74-,75-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,92-,93-,94-/m0/s1

InChI Key

OFIZOVDANLLTQD-ZVNXOKPXSA-N

Canonical SMILES

CCC(C)C(C(=O)NCC(=O)NC(CCCCN)C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CC(C)C)C(=O)NC(CC2=CN=CN2)C(=O)NC(CO)C(=O)NC(C)C(=O)NCC(=O)NC(CCCCN)C(=O)NC(CC3=CC=CC=C3)C(=O)NCC(=O)NC(CCCCN)C(=O)NC(C)C(=O)NC(CC4=CC=CC=C4)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)O)C(=O)NC(C(C)CC)C(=O)NC(CCSC)C(=O)NC(CCCCN)C(=O)NC(CO)C(=O)O)NC(=O)CN

1.Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method.

Watanabe H1, Kawano R. Anal Sci. 2016;32(1):57-60. doi: 10.2116/analsci.32.57.

This study describes the pore-forming properties of magainin 1 in planar lipid bilayers. These bilayers were prepared by the droplet contact method, which was executed on a microfabricated device for a high-throughput study. We arrayed four droplet chambers parallelly in the single device, and the current measurements were carried out simultaneously. Using this system, we measured the channel current conductance of magainin 1. We determined the pore size and the number of assembling monomers in magainin pores in mammalian and bacterial model membranes. This system is a powerful tool for analyzing transmembrane peptides and their antimicrobial activities.

2.Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes.

Zerweck J1, Strandberg E2, Bürck J2, Reichert J2, Wadhwani P2, Kukharenko O1, Ulrich AS3,4. Eur Biophys J. 2016 Apr 6. [Epub ahead of print]

PGLa and magainin 2 (MAG2) are amphiphilic α-helical frog peptides with synergistic antimicrobial activity. In vesicle leakage assays we observed the strongest synergy for equimolar mixtures of PGLa and MAG2. This result was consistent with solid-state 15N-NMR data on the helix alignment in model membranes. The Hill coefficients determined from the vesicle leakage data showed that the heterodimeric (PGLa-MAG2) interactions were stronger than the homodimeric (PGLa-PGLa and MAG2-MAG2) interactions. This result was also reflected in the free energy of dimerization determined from oriented circular dichroism and quantitative solid-state 19F-NMR analysis.

3.Preparation of bioactive and antimicrobial PLGA membranes by magainin II/EGF functionalization.

Yüksel E1, Karakeçili A2, Demirtaş TT3, Gümüşderelioğlu M4. Int J Biol Macromol. 2016 May;86:162-8. doi: 10.1016/j.ijbiomac.2016.01.061. Epub 2016 Jan 21.

Development of dual functional materials that are capable of both reducing bacterial interaction and encouraging host tissue integration has gained importance in design of biomaterials. In this study, we prepared a bilayer poly (lactide co-glycolide) fibrous membrane with antibacterial and bioactive properties by electrospinning. The antibacterial layer was produced by covalent immobilization of antimicrobial peptide, Magainin II. The bioactive layer incorporating epidermal growth factor (EGF) molecules was subsequently electrospun on the antibacterial layer. The membranes were characterized by X-ray photoelectron spectroscopy, scanning electron microscopy and fluorescence microscopy. EGF release was detected by enzyme-linked immunosorbent assay. The antibacterial activity was tested against Escherichia coli (E. coli) and Staphylococcus aureus (S. aureus). The ability to support tissue cell integration was detected by using L-929 mouse fibroblasts.

4.Pore Structure and Synergy in Antimicrobial Peptides of the Magainin Family.

Pino-Angeles A1, Leveritt JM 3rd1, Lazaridis T1. PLoS Comput Biol. 2016 Jan 4;12(1):e1004570. doi: 10.1371/journal.pcbi.1004570. eCollection 2016.

Magainin 2 and PGLa are among the best-studied cationic antimicrobial peptides. They bind preferentially to negatively charged membranes and apparently cause their disruption by the formation of transmembrane pores, whose detailed structure is still unclear. Here we report the results of 5-9 μs all-atom molecular dynamics simulations starting from tetrameric transmembrane helical bundles of these two peptides, as well as their stoichiometric mixture, and the analog MG-H2 in DMPC or 3:1 DMPC/DMPG membranes. The simulations produce pore structures that appear converged, although some effect of the starting peptide arrangement (parallel vs. antiparallel) is still observed on this timescale. The peptides remain mostly helical and adopt tilted orientations. The calculated tilt angles for PGLa are in excellent agreement with recent solid state NMR experiments. The antiparallel dimer structure in the magainin 2 simulations resembles previously determined NMR and crystal structures.