Dihydrosomatostatin incorporates a reduced peptide backbone that influences conformational rigidity and stability. Residue diversity supports investigations of binding dynamics, folding behavior, and solvent interactions. Researchers examine its structural transitions to understand hydrogen-bond networks. Use spans peptide analog design, structural modeling, and signaling-pathway exploration.
CAT No: R2646
CAS No:40958-31-4
Synonyms/Alias:Dihydrosomatostatin;Somatostatin-14 (reduced);40958-31-4;Somatostatin (15-28);Somatostatin (sheep reduced);DTXSID00193961;SCHEMBL11592550;SCHEMBL25286356;Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys;DTXCID40116452;HY-P4917;DA-67693;FS109331;CS-0674980;NS00126763;H-Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH;H-Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH; H-AGCKNFFWKTFTSC-OH;Somatostatin-14 (reduced) (H-Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH);
Dihydrosomatostatin is a synthetic peptide analogue structurally related to the endogenous neuropeptide somatostatin, distinguished by the reduction of one or more double bonds within its amino acid sequence. As a member of the somatostatin peptide family, it retains key features associated with receptor binding and biological activity, making it a valuable molecular tool for probing peptide-receptor interactions and signaling pathways. Its modified structure can confer altered metabolic stability and receptor selectivity, offering unique advantages for researchers investigating neuroendocrine regulation, peptide pharmacology, and cellular signaling. The compound's relevance extends across multiple areas of biochemical and physiological research, where it serves as a precise probe for dissecting the mechanisms underlying somatostatin-mediated processes.
Receptor Binding Studies: Dihydrosomatostatin is frequently employed in receptor binding assays to evaluate its affinity and selectivity for somatostatin receptor subtypes. The structural modifications present in this analogue allow researchers to systematically investigate the role of specific peptide features in receptor-ligand interactions. By comparing its binding kinetics and receptor subtype preferences to those of native somatostatin, scientists can elucidate the molecular determinants of receptor specificity, which is essential for advancing our understanding of neuropeptide signaling and the development of receptor-targeted agents.
Peptide Structure-Activity Relationship Analysis: The compound's modified backbone makes it an important reference molecule for structure-activity relationship (SAR) studies in peptide research. By incorporating dihydrosomatostatin into experimental frameworks, investigators can assess how subtle changes in peptide conformation influence biological activity, receptor activation, and downstream signaling events. Such analyses are crucial for mapping the functional domains of neuropeptides and for guiding the rational design of novel analogues with tailored pharmacological profiles.
Neuroendocrine Function Research: Due to its close resemblance to endogenous somatostatin, dihydrosomatostatin is utilized in studies focused on neuroendocrine regulation. Researchers deploy this peptide in in vitro and ex vivo systems to probe the modulation of hormone secretion, neurotransmitter release, and synaptic plasticity. Its unique properties may reveal insights into the physiological roles of somatostatin analogues, helping to distinguish between receptor subtypes and signaling mechanisms implicated in the control of endocrine and neuronal processes.
Peptide Stability and Metabolic Profiling: The reduction of double bonds within dihydrosomatostatin's structure can confer enhanced resistance to enzymatic degradation compared to its parent peptide. This characteristic is exploited in biochemical assays designed to assess peptide stability, metabolic fate, and degradation pathways. By monitoring the breakdown and persistence of this analogue under various experimental conditions, researchers gain a deeper understanding of the factors influencing peptide half-life and bioavailability, which is vital for the development of more robust research tools and potential future analogues.
Analytical Method Development: Dihydrosomatostatin also serves as a standard or reference compound in the development and validation of analytical techniques for peptide detection and quantification. Its defined chemical properties and stability profile make it suitable for optimizing chromatographic, spectrometric, or immunoassay-based methods. Accurate measurement of peptide analogues is essential for quality control, pharmacokinetic investigations, and the establishment of reproducible research protocols in peptide science.
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