The isolation and characterization of venom peptides are essential to gain insight into the pathophysiology of the active ingredients in venom and to improve the treatment of various diseases. At the same time, venom peptides also provide a new way to understand cellular and molecular pathways. Creative Biolabs has been committed to the development and research of venom peptides, providing reliable technical support and high-quality services for the isolation and characterization of your venom peptides through our professional platform and novel technologies.

Structure of Venom Peptides

Studies have shown that the main components of animal venom are enzymes, non-enzymatic proteins, and peptides. Many of these venom peptides can target a variety of ion channels, membrane transporters, and receptors. Venom peptides exhibit higher specificity and efficacy for targets than traditional small-molecule drugs.

Peptides and proteins, the main active components in animal venom, contain poly-pairs of disulfide bonds. Long-term selective pressures and co-evolutionary processes have led to significant structural diversity. The number of disulfide bonds varies in different animal venoms, for example, 40-80 residues are found in scorpions and snakes, while 10-40 cysteine residues are found in snails.

Fig.1 The number of peptides in different animals.¹

Isolation and Characterization of Venom Peptides

• Activity-based biochemical and chromatographic separation

Creative Biolabs offers different isolation methods based on the different properties of venom peptides.

Target-assisted identification technology can achieve high-throughput quantitative identification and significantly improve the efficiency and accuracy of natural product target identification, and common methods include stable isotope labeling by amino acids in cell culture (SILC) and isobaric tags for relative and absolute quantification (ITRAQ), tandem mass tag (TMT).

Published Data

Below are some figures from published articles on peptide isolation and purification:

Fig.2 Gel electrophoresis was used to determine the peptide content in the venom.²

Fig.3 Fractionate the venom using C18 RP-HPLC chromatography.²

• Native peptidome identification based on high-resolution mass spectrometry and transcriptome sequencing

In recent years, the rapid development and application of high-resolution mass spectrometry and gene sequencing technology have greatly broadened the breadth and depth of natural peptide research. Creative Biolabs offers a range of methods to help you identify peptides:

• Linear ion trap quadrupole–mass spectrometry (LTQ–MS)
• Quadrupole executive orbitrap (QE-orbitrap)
• Matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF)
• Electron spray ionization–mass spectrometer (ESI–MS), etc

Published Data

The following are some of the published figures on peptide identification:

Fig.4 MALDI-TOF mass spectrometry was used to determine venom peptide structure.²

Fig.5 Proteomics detection of peptides.²

If you have any questions about the isolation and identification of venom peptides, you can contact us now. Our dedicated venom peptide research team is here to help.

References

1. Chen, Na.; et al. "Animal protein toxins: origins and therapeutic applications." Biophysics reports. (2018): 233-242.
2. Walker, A.A.; et al. "Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar, Doratifera vulnerans." Proceedings of the National Academy of Sciences of the United States of America. (2021): e2023815118.

For Research Use Only | Not For Clinical Use