Product Name:Alytesin
CAS No:31078-12-3
Purity:95%
Molar Mass:1535.8
Chemical Formula:C68H106N22O17S
Storage:Store at -20 degrees Celsius
Sequence:XGRLGTQWAVGHLM
Application:Alytesin is a peptide originally isolated from the skin secretion of the midwife toad (Alytes obstetricans). This peptide, composed of 13 amino acids, is part of the bombesin-like peptide family and exhibits a range of biological activities, including stimulating the release of gastrointestinal hormones and modulating smooth muscle contraction. Alytesin's role in research is particularly relevant in studies investigating the physiological effects of bombesin-related peptides, making it a valuable tool for understanding receptor interactions, peptide signaling pathways, and potential therapeutic applications in gastrointestinal disorders.
Current Research:
Alytesin is a tetradecapeptide originally isolated from the skin secretions of the midwife toad, Alytes obstetricans. It belongs to the bombesin-like peptide family, which includes peptides such as bombesin and ranatensin. The primary structure of alytesin is Pyr-Gly-Arg-Leu-Gly-Thr-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2. Biological Activity Alytesin exhibits several pharmacological effects: Gastrointestinal Effects: It stimulates gastric acid secretion and induces contractions in intestinal smooth muscle. Cardiovascular Effects: Administration of alytesin leads to hypertension in vivo, as observed in canine studies. Thermoregulatory Effects: Central administration of alytesin modulates thermoregulation, indicating its role in body temperature control. Structural Characteristics Alytesin shares significant structural similarity with other bombesin-like peptides, particularly bombesin. Both peptides consist of 14 amino acids and exhibit analogous biological activities, suggesting a conserved mechanism of action among this peptide family. Evolutionary Perspective The presence of alytesin in Alytes obstetricans underscores the evolutionary conservation of bombesin-like peptides across amphibian species. This conservation suggests that these peptides play fundamental roles in physiological processes, such as regulating smooth muscle activity and maintaining homeostasis. Research Implications The study of alytesin and related peptides provides valuable insights into the physiological functions of bombesin-like peptides. Understanding their mechanisms can inform the development of therapeutic agents targeting related human receptors, potentially addressing conditions like gastrointestinal disorders and hypertension. In summary, alytesin is a bombesin-like peptide with diverse biological activities, including modulation of gastrointestinal function, cardiovascular regulation, and thermoregulation. Its structural and functional characteristics make it a significant subject in the study of peptide biology and pharmacology.
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