Magainin 1
(Synonyms: 蛙皮素 1; Magainin I) 目录号 : GC32312Magainin1是在非洲爪蟾皮肤中发现的抗微生物多肽。
Cas No.:108433-99-4
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Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis.
Magainin 1 kill bacteria by permeabilizing the cell membranes without exhibiting significant toxicity against mammalian cells. The main target of the peptide is considered to be the lipid matrix of the membranes[1]. Magainin 1 and 2 have a similar amino-acid sequence. Magainin 2 has higher antimicrobial activity than magainin 1[2]. Magainin 1 interacts with acidic lipids through electrostatic interactions followed by hydrophobic interactions to form an amphiphilic helix, inducing the leakage. Magainin 1 induces the leakage of calcein specifically out of negatively-charged vesicles. The peptide binds to bovine brain phosphatidylserine sonicated vesicles according to the Langmuir isotherm with a binding constant of 3.8×105 M-1 and a binding-site number of 0.10 per lipid molecule[3]. Magainin 2 displays antibiotic activity against numerous Gram-negative and Gram-positive bacteria. A similar spectrum of activity is seen on assay of magainin 1[4].
[1]. Matsuzaki K, et al. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta. 1998 Nov 10;1376(3):391-400. [2]. Watanabe H, et al. Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method. Anal Sci. 2016;32(1):57-60. [3]. Matsuzaki K, et al. Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles. Biochim Biophys Acta. 1989 May 19;981(1):130-4. [4]. Zasloff M, et al. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-53.
Cas No. | 108433-99-4 | SDF | |
别名 | 蛙皮素 1; Magainin I | ||
Canonical SMILES | Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser | ||
分子式 | C112H177N29O28S | 分子量 | 2409.85 |
溶解度 | H2O : 100 mg/mL (41.50 mM; Need ultrasonic) | 储存条件 | Store at -20°C |
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Atomic force spectroscopy with Magainin 1 functionalized tips and biomimetic supported lipid membranes
Eur Biophys J 2022 Jan;51(1):29-40.PMID:35031815DOI:10.1007/s00249-021-01580-y.
Antimicrobial peptides are molecules synthesized by living organisms as the first line of defense against bacteria, fungi, parasites, or viruses. Since their biological activity is based on destabilization of the microbial membranes, a study of direct interaction forces between antimicrobial peptides and biomimetic membranes is very important for understanding the molecular mechanisms of their action. Herein, we use atomic force spectroscopy to probe the interaction between atomic force microscopy (AFM) tips functionalized with Magainin 1 and supported lipid bilayers (SLBs) mimicking electrically uncharged membranes of normal eukaryotic cells and negatively charged membranes of bacterial cells. The investigations performed on negatively charged SLBs showed that the Magainin 1 functionalized AFM tips are quickly adsorbed into the SLBs when they approach, while they adhere strongly to the lipid membrane when retracted. On contrary, same investigations performed on neutral SLBs showed mechanical resistance of the lipid membrane to the tip breakthrough and negligible adhesion force at detachment.
Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles
Biochim Biophys Acta 1989 May 19;981(1):130-4.PMID:2719968DOI:10.1016/0005-2736(89)90090-4.
Effects of Magainin 1, a novel antimicrobial peptide, on the permeability of lipid vesicles were investigated by using calcein as a trapped fluorescent marker. Magainin 1 induces the leakage of calcein specifically out of negatively-charged vesicles. The peptide binds to bovine brain phosphatidylserine sonicated vesicles according to the Langmuir isotherm with a binding constant of 3.8.10(5) M-1 and a binding-site number of 0.10 per lipid molecule. The leakage seems to occur at a critical binding number of approx. 0.03 per lipid molecule. A circular dichroism study revealed that Magainin 1 conforms mainly to an unordered structure both in an aqueous solution and in the presence of egg yolk phosphatidylcholine vesicles, whereas to an amphiphilic helix with the phosphatidylserine vesicles. In conclusion, Magainin 1 interacts with acidic lipids through electrostatic interactions followed by hydrophobic interactions to form an amphiphilic helix, inducing the leakage.
Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method
Anal Sci 2016;32(1):57-60.PMID:26753706DOI: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.
In vitro biological activities of magainin alone or in combination with nisin
Peptides 2006 Jun;27(6):1201-9.PMID:16356589DOI:10.1016/j.peptides.2005.11.008.
Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells. Cells were cultured in presence of either nisin or Magainin 1 as well as in combination with both nisin and Magainin 1. Results have revealed that magainin, but not nisin, produces a loss of cell viability in HL-60 cells, and a minor increase of hemolysis, whereas it is not responsible for cell membrane disruption and lactate dehydrogenase (LDH) leakage. In addition, magainin is involved in a significant generation of reactive oxygen species (ROS), as well as in an augment of caspase-3 activity. Magainin-induced apoptosis was verified by DNA fragmentation and annexin V-FITC/propidium iodide (PI) staining of the cells. Promotion of cell death by magainin occurs via cytochrome c release accompanied by a substantial increase of proteasome activity. These results underline the importance of magainin as a drug capable of exerting an in vitro antitumoral activity by triggering apoptosis.
Magainin 2, a natural antibiotic from frog skin, forms ion channels in lipid bilayer membranes
Eur J Pharmacol 1992 Aug 3;226(4):287-96.PMID:1383011DOI:10.1016/0922-4106(92)90045-w.
We have examined the ion channel forming properties of magainin 2 by incorporating the peptide into artificial lipid bilayers held under voltage clamp. Magainin 2 increased lipid bilayer conductance in a concentration dependent manner with a Hill coefficient of 1.7. The magainin 2 conductance was selective for monovalent cations over anions with a ratio of 5:1 and had both voltage-sensitive and -insensitive components. Two structurally related but antibiotically less potent analogues, Magainin 1 and Z-12, also increased lipid bilayer conductance with a similar ion selectivity but these peptides were less potent than magainin 2. We propose that the weak cation selectivity of the magainin channels can be accounted for by the inclusion of negatively charged lipids in the channel complex and suggest two possible structures for such a channel. The ionophoric properties of these peptides are likely to be proximal to their antibiotic activities.