Eumenine mastoparan-ER
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Eumenine mastoparan-ER

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Eumenine mastoparan-ER is a linear cationic alpha-helical peptide that acts as an antimicrobial peptide by forming pore in membrane. It has antibacterial activity against both Gram-positive and Gram-negative strains. Eumenine mastoparan-ER has more potent activities against the yeast C.albicans. It shows moderate mast cell degranulation and leishmanicidal activities and has a very low hemolytic activity.

Category
Functional Peptides
Catalog number
BAT-012267
Synonyms
EMP-ER
Sequence
FDIMGLIKKVAGAL
1. Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes
Marcia Perez Dos Santos Cabrera, Marisa Rangel, João Ruggiero Neto, Katsuhiro Konno Toxins (Basel). 2019 Sep 24;11(10):559. doi: 10.3390/toxins11100559.
Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.
2. New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado
Katsuhiro Konno, et al. Toxins (Basel). 2019 Mar 10;11(3):155. doi: 10.3390/toxins11030155.
Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH₂) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH₂), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes.
3. First Comprehensive Analysis of Both Mitochondrial Characteristics and Mitogenome-Based Phylogenetics in the Subfamily Eumeninae (Hymenoptera: Vespidae)
Li Luo, James M Carpenter, Bin Chen, Tingjing Li Insects. 2022 Jun 8;13(6):529. doi: 10.3390/insects13060529.
The subfamily Eumeninae plays a significant role in the biological control of agricultural pests. However, the characteristics of eumenine mitogenomes that are important molecular markers for phylogenetics are not clearly revealed. Here, 52 eumenine mitogenomes are newly sequenced and annotated, and the phylogenetic relationships of the subfamily are comprehensively analyzed based on 87 vespid mitogenomes. Through the comparative analysis of the 54 eumenine mitogenomes, the gene compositions of about one half of the 54 species match with ancestral insect mitogenome, and remaining others contain two trnM which are highly similar, with 51.86% (Eumenes tripunctatus) to 90.65% (Pseumenes nigripectus) sequence identities, which is unique among the reported mitogenomes of the family Vespidae. Moreover, the translocation trnL1 upstream of nad1 is a common rearrangement event in all eumenine mitogenomes. The results of phylogenetic analyses support the paraphyly of the subfamily Eumeninae and the tribe Odynerini, respectively, and the monophyly of the tribe Eumenini, and verify that the tribe Zethini is a valid subfamily Zethinae. In this study, the relationships between some genera such as Allorhynchium and Pararrhynchium or the taxonomic status of the subgenera such as Eremodynerus and Dirhynchium are found to be confusing and there should be further inquiry with more samples.
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