Need Assistance?
  • US & Canada:
    +
  • UK: +

Alyteserin-1Mb

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

Alyteserin-1Mb is an antimicrobial peptide produced by Alytes maurus (Midwife toad). It has antibacterial and antifungal activity. It is active against Gram-negative bacterium: Escherichia coli NCTC 10418 (MIC=217 µM) and Gram-positive bacterium: Staphylococcus aureus NCTC 10788 (MIC=434 µM).

Category
Functional Peptides
Catalog number
BAT-013235
Molecular Formula
C106H178N30O27
Molecular Weight
2304.77
Synonyms
Gly-Phe-Lys-Glu-Val-Leu-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-Gly-Ile-Pro-Ala-His-Val-Ala-Asn-NH2
Purity
≥97%
Sequence
GFKEVLKAGLGSLVKGIPAHVAN-NH2
Storage
Store at -20°C
1. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent
J Michael Conlon, Milena Mechkarska, Manju Prajeep, Kholoud Arafat, Milan Zaric, Miodrag L Lukic, Samir Attoub Amino Acids. 2013 Feb;44(2):715-23. doi: 10.1007/s00726-012-1395-7. Epub 2012 Sep 11.
Alyteserin-2a (ILGKLLSTAAGLLSNL.NH(2)) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad Alytes obstetricans. Structure-activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the hydrophobic face of the helix were replaced by L-tryptophan and amino acids on the hydrophilic face were replaced by one or more L-lysine or D-lysine residues. The Trp-containing peptides display increased cytotoxic activity against non-small cell lung adenocarcinoma A549 cells (up to 11-fold), but hemolytic activity against human erythrocytes increases in parallel. The potency of the N15K analog against A549 cells (LC(50) = 13 μM) increases sixfold relative to alyteserin-2a and the therapeutic index (ratio of LC(50) for erythrocytes and tumor cells) increases twofold. Incorporation of a D-Lys(11) residue into the N15K analog generates a peptide that retains potency against A549 cells (LC(50) = 15 μM) but whose therapeutic index is 13-fold elevated relative to the native peptide. [G11k, N15K] alyteserin-2a is also active against human hepatocarcinoma HepG2 cells (LC(50) = 26 μM), breast adenocarcinoma MDA-MB-231 cells (LC(50) = 20 μM), and colorectal adenocarcinoma HT-29 cells (LC(50) = 28 μM). [G11k, N15K] alyteserin-2a, in concentrations as low as 1 μg/mL, significantly (P < 0.05) inhibits the release of the immune-suppressive cytokines IL-10 and TGF-β from unstimulated and concanavalin A-stimulated peripheral blood mononuclear cells. The data suggest a strategy of increasing the cationicity while reducing the helicity of naturally occurring amphipathic α-helical peptides to generate analogs with improved cytotoxicity against tumor cells but decreased activity against non-neoplastic cells.
2. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae)
J Michael Conlon, Anni Demandt, Per F Nielsen, Jérôme Leprince, Hubert Vaudry, Douglas C Woodhams Peptides. 2009 Jun;30(6):1069-73. doi: 10.1016/j.peptides.2009.03.004. Epub 2009 Mar 24.
Two families of structurally related C-terminally alpha-amidated antimicrobial peptides have been identified in norepinephrine-stimulated skin secretions of the midwife toad Alytes obstetricans (Alytidae). The alyteserin-1 peptides (Gly-Leu-Lys-(Asp/Glu)-Ile-Phe-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-(Gly/Asn)-Ile-Ala-Ala-His-Val-Ala-(Asn/Ser).NH(2)) show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae. Alyteserin-2a (Ile-Leu-Gly-Lys-Leu-Leu-Ser-Thr-Ala-Ala-Gly-Leu-Leu-Ser-Asn-Leu.NH(2)) and alyteserin-2b and -2c (Ile-Leu-Gly-Ala-Ile-Leu-Pro-Leu-Val-Ser-Gly-Leu-Leu-Ser-(Asn/Ser)-Lys-Leu x NH(2)) show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae. The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacteria Escherichia coli (MIC=25 microM) whereas alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus (MIC=50 microM). The hemolytic activity against human erythrocytes of all peptides tested is relatively weak (LC(50)>100 microM). The data demonstrate that the frogs belonging to the family Alytidae are among those producing dermal antimicrobial peptides that may represent a component of the animal's system of innate immunity.
3. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides
Bin Gao, Patrick Sherman, Lan Luo, John Bowie, Shunyi Zhu FASEB J. 2009 Apr;23(4):1230-45. doi: 10.1096/fj.08-122317. Epub 2008 Dec 16.
Both vertebrates and invertebrates employ alpha-helical antimicrobial peptides (AMPs) as an essential component of their innate immune system. However, evolutionary relation of these immune molecules remains unresolved. Venoms, as key weapons of venomous arthropods for prey and defense, receive increasing recognition as an emerging source of such peptides. From a cDNA library prepared from the venom gland of the scorpion Mesobuthus eupeus, clones encoding precursors of two new AMPs, named meucin-13 (IFGAIAGLLKNIF-NH(2)) and meucin-18 (FFGHLFKLATKIIPSLFQ), have been isolated. The precursor of meucins consists of a signal peptide, a mature peptide, and an acidic propeptide, in which dibasic residues as the typical processing signal are located between the mature and propeptide. Meucin-13 is an ortholog of several previously described AMPs from scorpion venom and has also detectable sequence similarity to temporins, a large family of AMPs from frog skin, whereas meucin-18 displays some similarity to AMPs from diverse origin including arthropod venoms, fish mast cells, and frog skins. These two meucin peptides form alpha-helical structure in the presence of 50% trifluoroethanol (TFE), a membrane-mimicking environment, as identified by circular dichroism (CD) spectroscopy. This finding is further verified by their NMR structures that show a typical alpha-helical amphipathic design, a structural prerequisite for cytolytic activity. Meucins exhibit extensive cytolytic effects on both prokaryotic and eukaryotic cells (gram(+) and gram(-) bacteria, fungi, yeasts, rabbit erythrocytes, and rat dorsal root ganglion cells) at micromolar concentrations. It is remarkable that muecin-18 was 2- to >14-fold more potent than meucin-13 against nearly all the cells tested. Structural differences in hydrophilic/hydrophobic balance and cationic amino acid location between two meucins could account for their differential potency. Despite these differences, commonalities at precursor organization, three-dimensional structure, and biological function suggests that meucins are two evolutionarily related AMPs and likely originated from a common ancestor by gene duplication. Our work presented here also provides new insights into an evolutionary link among AMPs from invertebrates and vertebrates and clues for evolutionary convergence between AMPs and virus fusion domains.
Online Inquiry
Verification code
Inquiry Basket