Bombinakinin-GAP

Product Name:Bombinakinin-GAP

CAS No:573671-91-7

Purity:95%

Molar Mass:3228.75

Chemical Formula:C145H219N39O39S3

Storage:Store at -20 degrees Celsius

Sequence:DMYEIKQYKTAHGRPPICAPGEQCPIWV

Target:bradykinin-related peptide

Application:

Bombinakinin-GAP is a peptide derived from the skin secretions of Bombina frogs, belonging to the tachykinin family, known for roles in neurotransmission and smooth muscle contraction. Structurally similar to substance P, Bombinakinin-GAP influences physiological processes such as pain modulation, inflammation, and cardiovascular regulation. It interacts with neurokinin receptors, making it a valuable tool in research focused on the nervous and cardiovascular systems. Researchers use Bombinakinin-GAP to explore mechanisms underlying pain, inflammatory responses, and blood pressure control. This peptide's study aids in understanding neuropeptide signaling, offering potential insights for developing therapies for pain, inflammation, and hypertension.

Current Research:

Bombinakinin-GAP is a 28-amino acid peptide isolated from the skin secretions of the toad Bombina maxima. Its primary structure is DMYEIKQYKTAHGRPPICAPGEQCPIWV-NH2, featuring a disulfide bond between two cysteine residues. This peptide is classified as a bradykinin-related peptide (BRP), a group known for their diverse biological activities. Biological Activity In studies involving rats, intracerebroventricular administration of Bombinakinin-GAP resulted in a significant reduction in food intake, indicating its potential role in appetite regulation. The exact mechanisms underlying this effect remain to be fully elucidated, but it suggests that Bombinakinin-GAP may influence central pathways involved in feeding behavior. Research Applications Due to its unique structure and biological activity, Bombinakinin-GAP serves as a valuable tool in research focused on: Neuroscience: Investigating the central mechanisms of appetite control and the potential therapeutic applications for disorders related to feeding and metabolism. Pharmacology: Exploring the interactions of BRPs with their receptors and the subsequent physiological responses, which could inform drug development targeting related pathways. Comparative Physiology: Understanding the evolutionary significance and functional diversity of amphibian skin peptides, contributing to the broader knowledge of peptide biology across species. Handling and Storage For experimental use, Bombinakinin-GAP is typically supplied as a lyophilized powder. It is recommended to rehydrate the peptide immediately before use to ensure stability and activity. Unused portions should not be refrozen to maintain integrity. Specific storage conditions may vary depending on the supplier's guidelines. Conclusion Bombinakinin-GAP exemplifies the rich biochemical diversity found in amphibian skin secretions. Its ability to modulate feeding behavior in animal models highlights its potential as a subject for further research into appetite regulation and the development of novel therapeutic agents.

Reference:

Wang, L., Chen, Y., Yang, M., Zhou, M., Chen, T., Sui, D. Y., & Shaw, C. (2010). Peptide DV-28 amide: An inhibitor of bradykinin-induced arterial smooth muscle relaxation encoded by Bombina orientalis skin kininogen-2. Peptides, 31(5), 979-982.