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

Maximin H2

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

Maximin H2 has antibacterial and antifungal activities. The source of Maximin H2 is Bombina maxima [Giant fire-bellied toad]. It is highly homologous with bombinin H peptides.

Category
Functional Peptides
Catalog number
BAT-012020
Molecular Formula
C91H164N22O23S
Molecular Weight
1966.47
Purity
>97% by HPLC
Sequence
ILGPVLSMVGSALGGLIKKI
1. Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis
Chang Zhou, Zhengming Wang, Xin Peng, Yao Liu, Yangjun Lin, Zhe Zhang, Yuling Qiu, Meihua Jin, Ran Wang, Dexin Kong Chem Biol Drug Des. 2018 Jan;91(1):50-61. doi: 10.1111/cbdd.13055. Epub 2017 Jul 19.
Amphibian skin secretions are known to contain numerous peptides with a large array of biological activities. Bombinins are a group of amphibian-derived peptides with broad spectrum antimicrobial activities that have been only identified from the ancient toad species, Bombina. In this study, we described the identification and characterization of a novel bombinin precursor which encoded a bombinin-like peptide (BLP-7) and a novel bombinin H-type peptide (named as Bombinin H-BO) from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. The primary structures of both mature peptides were determined by combinations of molecular cloning of peptide precursor-encoding cDNAs and mass spectrometry techniques. Secondary structure prediction revealed that both peptides had cationic amphipathic α-helical structural features. The synthetic replicate of BLP-7 displayed more potent antimicrobial activity than Bombinin H-BO against Gram-positive and Gram-negative bacteria and yeast. Also, in vitro antitumour assay showed that both peptides possessed obvious antiproliferative activity on three human hepatoma cells (Hep G2/SK-HEP-1/Huh7) at the non-toxic doses. These results indicate the peptide family of bombinins could be a potential source of drug candidates for anti-infection and anticancer therapy.
2. An anionic antimicrobial peptide from toad Bombina maxima
Ren Lai, Hen Liu, Wen Hui Lee, Yun Zhang Biochem Biophys Res Commun. 2002 Jul 26;295(4):796-9. doi: 10.1016/s0006-291x(02)00762-3.
Amphibian skin is a rich resource of antimicrobial peptides like maximins and maximins H from toad Bombina maxima. A novel cDNA clone encoding a precursor protein that comprises maximin 3 and a novel peptide, named maximin H5, was isolated from a skin cDNA library of B. maxima. The predicted primary structure of maximin H5 is ILGPVLGLVSDTLDDVLGIL-NH2. Containing three aspartate residues and no basic amino acid residues, maximin H5 is characterized by an anionic property. Different from cationic maximin H peptides, only Gram-positive strain Staphylococcus aureus was sensitive to maximin H5, while the other bacterial and fungal strains tested were resistant to it. The presence of metal ions, like Zn2+ and Mg2+, did not increase its antimicrobial potency. Maximin H5 represents the first example of potential anionic antimicrobial peptides from amphibians. The results provide the first evidence that, together with cationic antimicrobial peptides, anionic antimicrobial peptides may also exist naturally as part of the innate defense system.
3. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima
Ting Wang, Jie Zhang, Ji-Hong Shen, Yang Jin, Wen-Hui Lee, Yun Zhang Biochem Biophys Res Commun. 2005 Feb 18;327(3):945-51. doi: 10.1016/j.bbrc.2004.12.094.
Amphibian skin secretions are rich in antimicrobial peptides acting as important components of innate defense system against invading microorganisms. A novel type of peptide, designated as maximin S, was deduced by random sequencing of 793 clones from a constructed Bombina maxima skin cDNA library. The putative primary structures of maximin S peptides can be grouped into five species, in which maximin S1 has 14 amino acid residues and the rest of maximin S peptides (S2-S5) all have 18 amino acid residues. Unlike most of the amphibian antimicrobial peptides so far identified, the newly characterized four maximin S precursors are composed of maximin S1 and different combinations of tandem repeated maximin S2-S5 linked by internal peptides. Except maximin S1, the predicted secondary structures of maximin S2-S5 show a similar amphipathic alpha-helical structure. MALDI-TOF mass spectrometry analysis of partially isolated skin secretions of the toad indicates that most of the deduced maximin S peptides are expressed. Two deduced maximin S peptides (S1, S4) were synthesized and their antimicrobial activities were tested. Maximin S4 only had an antibiotic activity against mycoplasma and had no antibacterial or antifungal activity toward tested strains. Maximin S1 had no activity under the same conditions.
Online Inquiry
Verification code
Inquiry Basket