Amylin, amide, rat is a potent and high affinity ligand of Amylin receptor AMY1 and AMY3 receptors and variably of AMY2 receptors; binding studies are generally used for the latter receptor.
CAT No: R1190
CAS No:124447-81-0
Synonyms/Alias:Amylin (rat);124447-81-0;Amylin (mouse, rat) trifluoroacetate salt;DA-50442;FA110436;PD077004;H-Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-Arg-Ser-Ser-Asn-Asn- Leu-Gly-Pro-Val-Leu-Pro-Pro-Thr-Asn-Val-G ly-Ser-Asn-Thr-Tyr-NH2; H-KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY-NH2;
Amylin, amide, rat is a synthetic peptide corresponding to the rat amylin sequence with a C-terminal amidation, a modification that closely mimics the native hormone as found in rodent species. As a 37-amino acid peptide, amylin is co-secreted with insulin from pancreatic beta cells and is a key regulator of glucose metabolism, satiety, and energy homeostasis. Its unique structure, including the disulfide bridge and amidated terminus, confers distinct biophysical properties that are relevant to its aggregation behavior and receptor interactions. In research settings, the rat form of amylin is widely utilized to investigate species-specific mechanisms of peptide action, amyloidogenesis, and metabolic regulation, making it an essential tool for both basic and applied biochemical studies.
Peptide aggregation studies: Amylin's propensity to form amyloid fibrils is a central focus in the investigation of protein misfolding and aggregation disorders. The rat variant, which differs from human amylin by several key residues, is significantly less amyloidogenic, making it a valuable comparative model for elucidating the structural determinants that govern peptide aggregation. Researchers employ synthetic rat amylin to characterize the molecular mechanisms underlying amyloid inhibition, to test the efficacy of anti-aggregation compounds, and to delineate species-dependent differences in fibrillogenesis.
Metabolic regulation research: The peptide is extensively used in metabolic and endocrinological studies to dissect the physiological roles of amylin in rodents. Its effects on glucose homeostasis, insulin secretion, and gastric emptying are of particular interest for understanding the integrated hormonal control of energy balance. Experimental administration of rat amylin, either in isolated islet preparations or in vivo models, enables detailed analysis of its signaling pathways, receptor interactions, and downstream metabolic consequences, providing insights into the peptide's contribution to glycemic regulation.
Receptor pharmacology: The availability of rat amylin, amide, facilitates studies on the pharmacodynamics and pharmacokinetics of amylin-receptor interactions. Using radioligand binding assays, functional cell-based assays, and receptor mutagenesis approaches, researchers can probe the specificity and affinity of amylin for its cognate receptors and receptor activity-modifying proteins (RAMPs). These studies are critical for mapping the molecular determinants of peptide-receptor recognition, understanding cross-species pharmacology, and developing novel peptide analogues with altered receptor selectivity.
Peptide structure-function analysis: Rat amylin serves as an important model for structure-activity relationship (SAR) investigations. By comparing the conformational properties, stability, and bioactivity of rat versus human or other species' amylins, scientists can identify sequence motifs responsible for biological activity and aggregation propensity. Such research leverages techniques including NMR spectroscopy, circular dichroism, and mass spectrometry to unravel the contributions of specific amino acid substitutions and post-translational modifications, such as C-terminal amidation, to overall peptide function.
Peptide synthesis and analytical validation: The synthetic rat amylin peptide is also employed as a reference standard in peptide synthesis, purification, and analytical quality control. Its defined sequence and well-characterized physicochemical properties make it suitable for calibrating chromatographic methods, validating mass spectrometric detection, and benchmarking peptide manufacturing processes. This utility supports the development of robust workflows for the production and characterization of bioactive peptides, ensuring reproducibility and reliability in peptide-based research and industrial applications.
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