Dermaseptin
(Synonyms: 皮抑菌肽) 目录号 : GC32347
Dermaseptin是从青蛙皮肤分离的多肽，对细菌，真菌和原生动物表现出有效的抗菌活性。
Cas No.:136212-91-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Dermaseptin, a peptide isolated from frog skin, exhibits potent antimicrobial activity against bacteria, fungi and protozoa.
Dermaseptin is a water-soluble, thermostable, and nonhemolytic peptide endowed with highly potent antimicrobial activity against pathogenic fungi at micromolar concentration. Circular dichroism spectra of dermaseptin in hydrophobic media indicated 80% alpha-helical conformation, and predictions of secondary structure suggested that dermaseptin can be configured as an amphiphatic alpha-helix spanning over residues 1-27, a structure that perturbs membrane functions regulating water flux[1]. Dermaseptin exerts a lytic action upon bacteria, protozoa, yeasts, and filamentous fungi at micromolar concentrations. Molecular elements responsible for the exceptional antimicrobial potency of dermaseptin are to be traced to the NH2-terminal alpha-helical amphipathic segment spanning residues 1-18 of the molecule[1].
[1]. Mor A, et al. Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry. 1991 Sep 10;30(36):8824-30. [2]. Mor A, et al. The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J Biol Chem. 1994 Jan 21;269(3):1934-9.
| Cas No. | 136212-91-4 | SDF | |
| 别名 | 皮抑菌肽 | ||
| Canonical SMILES | Ala-Leu-Trp-Lys-Thr-Met-Leu-Lys-Lys-Leu-Gly-Thr-Met-Ala-Leu-His-Ala-Gly-Lys-Ala-Ala-Leu-Gly-Ala-Ala-Ala-Asp-Thr-Ile-Ser-Gln-Gly-Thr-Gln | ||
| 分子式 | C152H257N43O44S2 | 分子量 | 3455.1 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.2894 mL | 1.4471 mL | 2.8943 mL |
| 5 mM | 0.0579 mL | 0.2894 mL | 0.5789 mL |
| 10 mM | 0.0289 mL | 0.1447 mL | 0.2894 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
The Dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides
Biochim Biophys Acta 2009 Aug;1788(8):1537-50.PMID:18929530DOI:10.1016/j.bbamem.2008.09.006.
Skin secretions of hylid frogs show amazing levels of interspecific and intraspecific diversity and are comprised of a cocktail of genetically-related, but markedly diverse antimicrobial peptides that are grouped into a superfamily, termed the dermaseptins, comprising several families: dermaseptins (sensu stricto), phylloseptins, plasticins, dermatoxins, phylloxins, hyposins, caerins, and aureins. Dermaseptin gene superfamily evolution is characterized by repeated gene duplications and focal hypermutations of the mature peptide coding sequence, followed by positive (diversifying) selection. We review here molecular mechanisms leading to these vast combinatorial peptide libraries, and structural and functional properties of antimicrobial peptides of the Dermaseptin and plasticin families, as well as those of Dermaseptin S9, an amyloidogenic peptide with antimicrobial and chemoattractant activities.
The Dermaseptin precursors: a protein family with a common preproregion and a variable C-terminal antimicrobial domain
FEBS Lett 1999 Aug 13;456(3):352-6.PMID:10462042DOI:10.1016/s0014-5793(99)00964-3.
Preprodermaseptins are a group of antimicrobial peptide precursors found in the skin of a variety of frog species. Precursors of this family have very similar N-terminal preprosequences followed by markedly different C-terminal domains that correspond to mature antimicrobial peptides. Some of these peptides are 24-34 amino acids long and form well-behaved amphipathic alpha-helices, others are disulfide-linked peptides of 20-46 residues, still others, highly hydrophobic, are the smallest antimicrobial peptides known so far being only 10-13 residues in length. All these peptides are broad-spectrum microbicides that kill many bacteria, protozoa, yeasts and fungi by destroying or permeating the microbial membrane. In frogs belonging to the genus Phyllomedusinae, preprodermaseptins encoded peptides also include dermorphins and deltorphins, D-amino acid-containing heptapeptides which are very potent and specific agonists of the mu- or delta-opioid receptors. The remarkable similarity between preproregions of precursors that give rise to peptides with very different primary structures, conformations and activities suggests that the corresponding genes originate from a common ancestor. The high conservation of the precursor prepropart indicates that this region must have an important function.
Effect of Dermaseptin on erythrocytes
Basic Clin Pharmacol Toxicol 2013 Nov;113(5):347-52.PMID:23841716DOI:10.1111/bcpt.12096.
Dermaseptin, an antimicrobial peptide participating in the host defence against pathogens, interacts with the membrane of target cells, leading to membrane permeabilization and eventual cell lysis. Dermaseptin has previously been shown to trigger haemolysis. Prior to haemolysis, erythrocytes may enter suicidal death or eryptosis, which is characterized by cell shrinkage and by cell membrane scrambling leading to phosphatidylserine exposure at the erythrocyte surface. Triggers of eryptosis include increase in cytosolic Ca虏鈦?activity [(Ca虏鈦?](i) and formation of ceramide. This study explored whether Dermaseptin modifies [Ca虏鈦篯(i) and elicits eryptosis. Cell volume has been estimated from forward scatter, phosphatidylserine exposure from annexin-V binding, haemolysis from haemoglobin release, ceramide formation from binding of fluorescent antibodies and [Ca虏鈦篯(i) from Fluo3-fluorescence. A 48-hr exposure to Dermaseptin (50 渭M) was followed by a significant increase in [Ca虏鈦篯(i), a significant increase ceramide abundance, a significant decrease in forward scatter and a significant increase in annexin-V binding. The annexin-V binding after Dermaseptin treatment was significantly blunted but not abrogated in the nominal absence of extracellular Ca虏鈦? Dermaseptin triggers eryptosis, an effect at least partially due to entry of extracellular Ca虏鈦?
Dermaseptin-PH: A Novel Peptide with Antimicrobial and Anticancer Activities from the Skin Secretion of the South American Orange-Legged Leaf Frog, Pithecopus (Phyllomedusa) hypochondrialis
Molecules 2017 Oct 24;22(10):1805.PMID:29064402DOI:10.3390/molecules22101805.
The Dermaseptin peptides, mainly derived from the skin secretions of Hylidae frogs, belong to a superfamily of antimicrobial peptides and exhibit diverse antimicrobial and anticancer activities with low cytotoxicity. Here, we reported a novel Dermaseptin peptide, from the South American orange-legged leaf frogs, Pithecopus (Phyllomedusa) hypochondrialis, processing the shortest peptide length, namely Dermaseptin-PH. The complementary DNA (cDNA) encoding biosynthetic precursor of Dermaseptin-PH was initially identified by the rapid amplification of cDNA ends PCR (RACE-PCR) technique from the skin secretion. The predicted primary structure was confirmed by a combination of reverse-phase high performance liquid chromatography (RP-HPLC) and MS/MS fragmentation from the skin secretion. Chemically-synthetic Dermaseptin-PH was investigated using a range of bioactivity assessment assays to evaluate the biological activities and cytotoxicity of Dermaseptin-PH. Dermaseptin-PH inhibited the growth of Gram-negative bacteria, Gram-positive bacteria, and pathogenic yeast Candidaalbicans. In addition, Dermaseptin-PH showed a broad-spectrum of anticancer activities against several cancer cell lines including MCF-7, H157, U251MG, MDA-MB-435S, and PC-3. The potent antimicrobial and anticancer activities of Dermaseptin-PH make it a promising candidate in the discovery of new drugs for clinical applications, and the relatively short sequence of Dermaseptin-PH can provide new insight for the research and structural modification of new peptide drugs.
Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
Toxins (Basel) 2016 May 12;8(5):144.PMID:27187467DOI:10.3390/toxins8050144.
The Dermaseptin antimicrobial peptide family contains members of 27-34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs. By use of a degenerate primer in Rapid amplification of cDNA ends (RACE) PCR designed to a common conserved domain within the 5'-untranslated regions of previously-characterized Dermaseptin encoding cDNAs, two novel members of this peptide family, named dermaseptin-PD-1 and dermaseptin-PD-2, were identified in the skin secretion of the phyllomedusine frog, Pachymedusa dacnicolor. The primary structures of both peptides were predicted from cloned cDNAs, as well as being confirmed by mass spectral analysis of crude skin secretion fractions resulted from reversed-phase high-performance liquid chromatography. Chemically-synthesized replicates of dermaseptin-PD-1 and dermaseptin-PD-2 were investigated for antimicrobial activity using standard model microorganisms (Gram-positive bacteria, Gram-negative bacteria and a yeast) and for cytotoxicity using mammalian red blood cells. The possibility of synergistic effects between the two peptides and their anti-cancer cell proliferation activities were assessed. The peptides exhibited moderate to high inhibition against the growth of the tested microorganisms and cancer cell lines with low haemolytic activity. Synergistic interaction between the two peptides in inhibiting the proliferation of Escherichia coli and human neuronal glioblastoma cell line, U251MG was also manifested.