Guanylin (human) is a cysteine-rich peptide containing two disulfide bonds that stabilize β-sheet-like architecture. The sequence supports studies of redox behavior, folding pathways, and metal interactions. Researchers examine its conformational shifts and receptor-binding motifs. Its structural rigidity makes it suitable for detailed biophysical mapping.
CAT No: R2228
CAS No:183200-12-6
Synonyms/Alias:Guanylin (human);183200-12-6;Guanylin(human);Guanylin, human;MFCD00187933;AKOS024456838;DA-73944;FG108840;PD079197;H-Pro-Gly-Thr-Cys-Glu-Ile-Cys-Ala-Tyr-Ala-Ala-Cys-Thr-Gly-Cys-OH; H-PGTCEICAYAACTGC-OH;
Guanylin (human) is a naturally occurring peptide hormone that plays a pivotal role in the regulation of electrolyte and water transport in the gastrointestinal tract. As a member of the guanylin family of peptides, it functions primarily by activating guanylate cyclase-C (GC-C) receptors on the surface of intestinal epithelial cells, leading to increased intracellular cyclic GMP levels. This biochemical mechanism underpins its fundamental involvement in fluid homeostasis, intestinal secretion, and modulation of epithelial cell signaling. The peptide's significance extends to various research domains, including gastrointestinal physiology, peptide-receptor interactions, and cellular signaling pathways relevant to mucosal biology.
Receptor binding studies: Guanylin serves as an important ligand in investigations focused on GC-C receptor activation and downstream signaling cascades. By enabling researchers to probe the specificity, affinity, and structural determinants of peptide-receptor interactions, it facilitates a deeper understanding of cyclic GMP-mediated processes in epithelial cells. Such studies are instrumental in elucidating the molecular basis of intestinal ion transport and barrier function, as well as in identifying potential modulators of GC-C activity.
Signal transduction research: The peptide is widely utilized in experimental models to dissect the intricacies of cyclic GMP-dependent signaling pathways within gastrointestinal tissues. Its ability to stimulate GC-C receptors allows for precise characterization of second messenger systems, cross-talk with other intracellular signaling networks, and the effects of altered cyclic GMP levels on cellular physiology. These insights are particularly valuable for advancing knowledge of intestinal homeostasis and the biochemical regulation of fluid secretion.
Intestinal physiology modeling: In vitro and ex vivo systems frequently employ guanylin to mimic endogenous regulatory mechanisms governing salt and water exchange across the intestinal epithelium. By providing a physiologically relevant stimulus, the peptide aids in the assessment of epithelial transport function, permeability, and the adaptive responses of mucosal tissues to environmental or pharmacological challenges. Such applications are critical for the development of high-fidelity models of gastrointestinal function and for the evaluation of potential interventions targeting epithelial health.
Peptide structure-function analysis: As a well-characterized bioactive peptide, guanylin is an excellent model for structure-activity relationship (SAR) studies. Researchers leverage its defined sequence and biological activity to investigate the impact of specific amino acid substitutions, peptide modifications, or conformational changes on receptor activation and biological efficacy. These structure-function investigations contribute to the rational design of novel peptide analogs and deepen understanding of the molecular features essential for biological activity.
Analytical method development: Guanylin is also employed as a reference standard or analytical target in the development and validation of detection methods for peptide hormones in biological samples. Its use supports the optimization of chromatographic, immunoassay, and mass spectrometry-based techniques, enabling accurate quantification and monitoring of peptide levels in complex matrices. These analytical applications are integral to advancing peptide biochemistry and supporting high-quality research in gastrointestinal and endocrine biology.
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