HAEGTFTSD is the first N-terminal 1-9 residues of GLP-1 peptide.
CAT No: R1408
CAS No:926018-45-3
Synonyms/Alias:HAEGTFTSD;926018-45-3;BMB01845;HY-P1226;CS-8036;DA-53816;MS-31809;G16250;(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3R)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]propanoyl]amino]-4-carboxybutanoyl]amino]acetyl]amino]-3-hydroxybutanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]butanedioic acid;
HAEGTFTSD is a synthetic peptide corresponding to the N-terminal fragment of human glucagon-like peptide-1 (GLP-1), a key incretin hormone involved in the regulation of glucose metabolism and insulin secretion. As a bioactive peptide, it is of significant interest in the field of endocrinology and metabolic research, particularly for its role in mimicking or modulating peptide hormone activity. Its sequence allows for the study of peptide-receptor interactions, peptide degradation pathways, and the structural determinants of biological activity. Researchers utilize this fragment to dissect the mechanisms of GLP-1 signaling and to develop novel peptide analogs for experimental applications.
Peptide-receptor interaction studies: HAEGTFTSD serves as a valuable tool in analyzing the binding affinity and specificity of GLP-1 receptor-ligand interactions. By employing this peptide fragment in receptor binding assays, researchers can elucidate the minimal sequence requirements for receptor activation or antagonism. Such studies provide insights into the structural motifs necessary for effective receptor engagement, supporting the rational design of next-generation peptide ligands with improved selectivity or altered signaling profiles.
Enzymatic degradation assays: The peptide's defined sequence makes it ideal for investigating the enzymatic pathways responsible for GLP-1 inactivation, such as dipeptidyl peptidase-4 (DPP-4) mediated cleavage. Utilizing HAEGTFTSD in controlled in vitro experiments enables detailed characterization of substrate recognition, cleavage kinetics, and the influence of sequence modifications on peptide stability. These findings are critical for understanding peptide half-life and turnover in physiological and experimental settings.
Peptide synthesis and analog development: As a representative N-terminal fragment, HAEGTFTSD is frequently used as a template for the development and optimization of synthetic peptide analogs. Researchers leverage its sequence to explore structure-activity relationships, assess the impact of amino acid substitutions, and generate modified peptides with tailored biological properties. This approach supports the advancement of peptide-based research tools and experimental probes for signaling studies.
Structural and conformational analysis: The defined primary structure of HAEGTFTSD enables its use in studies of peptide folding, secondary structure formation, and conformational dynamics. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and computational modeling benefit from this peptide's tractable size and well-characterized sequence. Such analyses contribute to a deeper understanding of the relationship between peptide structure and function, informing both basic and applied peptide science.
Signal transduction research: Employing HAEGTFTSD in cell-based assays or biochemical systems allows for the dissection of downstream signaling events initiated by GLP-1 receptor activation. By isolating the N-terminal region's contribution to receptor engagement, researchers can map specific signaling cascades, evaluate the impact of peptide modifications on intracellular responses, and identify novel regulatory mechanisms. These studies are instrumental in advancing knowledge of peptide hormone signaling and its broader physiological implications.
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