Splenopentin exhibits the full bioactivity of the hormone splenin. Splenopentin increases white blood-cell production if suppressed, in addition to other immune-regulating compounds, which includes interleukin-3 and macrophage colony-stimulating factors.
CAT No: 10-101-41
CAS No:75957-60-7 (net), 105184-37-0 (acetate)
Synonyms/Alias:Splenopentin Acetate;105184-37-0;acetic acid;4-[[6-amino-2-[[2-amino-5-(diaminomethylideneamino)pentanoyl]amino]hexanoyl]amino]-5-[[1-[[1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid;
Splenopentin Acetate is a synthetic pentapeptide that represents a biologically active fragment derived from splenin, a spleen-derived immunomodulatory peptide. As a member of the peptide compound class, it is composed of the amino acid sequence Arg-Lys-Glu-Val-Tyr, and is frequently studied for its capacity to mimic or modulate immunological processes in vitro and in vivo. Its well-defined sequence and stability in acetate salt form make it a valuable tool for researchers investigating the molecular mechanisms underlying immune cell regulation, peptide-receptor interactions, and the broader landscape of immunopharmacology. The unique bioactivity profile and structural simplicity of Splenopentin Acetate have positioned it as a model peptide for exploring immune-related pathways and developing peptide-based research tools.
Immunological research: Splenopentin Acetate is widely utilized in immunology laboratories to elucidate mechanisms of immune modulation at the cellular and molecular levels. Its ability to interact with immune cell populations, particularly T lymphocytes, makes it an essential probe for dissecting signaling cascades and functional responses associated with immune activation and suppression. Researchers leverage its structural analogy to endogenous splenin to probe the functional consequences of peptide-mediated immune regulation, facilitating the identification of novel targets and pathways involved in immune homeostasis.
Peptide-receptor interaction studies: The defined sequence of Splenopentin Acetate enables precise investigations into peptide-receptor binding dynamics. It serves as a reference molecule for mapping ligand-receptor interactions, determining binding affinities, and characterizing downstream signaling events in cell-based assays. Such studies are critical for understanding the specificity and selectivity of peptide ligands in modulating cellular responses, and for elucidating the molecular underpinnings of peptide-mediated communication within the immune system.
Peptide synthesis and analog development: The straightforward structure of Splenopentin Acetate renders it an ideal starting point for the synthesis of peptide analogs and derivatives. Researchers employ it as a template for structure-activity relationship (SAR) studies, systematically modifying amino acid residues to assess the impact on biological activity, stability, and receptor engagement. These efforts support the rational design of novel immunomodulatory peptides and expand the toolkit for probing structure-function relationships in immunopeptides.
In vitro assay development: Splenopentin Acetate is frequently incorporated into in vitro assay systems designed to monitor immune cell function, cytokine release, or signal transduction events. Its reproducible activity profile provides a reliable positive control or reference standard in experimental workflows, enabling the validation of assay sensitivity, specificity, and reproducibility. The use of this peptide in assay development supports the generation of robust, high-throughput screening platforms for immunological research.
Biochemical mechanism elucidation: The peptide's defined sequence and immunological relevance make it a valuable molecular probe for dissecting the biochemical mechanisms underlying spleen-derived peptide activity. By employing Splenopentin Acetate in mechanistic studies, researchers can investigate the role of specific amino acid motifs in modulating protein-protein interactions, enzyme activation, and intracellular signaling. These insights contribute to a deeper understanding of how small peptides influence complex biological systems, informing the future development of peptide-based research tools and reagents.
Splenopentin (SP-5, Arg-Lys-Glu-Val-Tyr) and thymopentin (TP-5, Arg-Lys-Asp-Val-Tyr) are synthetic immunomodulating peptides corresponding to the region 32-34 of a splenic product called splenin (SP) and the thymic hormone thymopoietin (TP), respectively. TP was originally isolated as a 5-kDa (49-amino acids) protein from bovine thymus while studying effects of the thymic extracts on neuromuscular transmission and was subsequently observed to affect T cell differentiation and function. TP I and II are two closely related polypeptides isolated from bovine thymus. A radioimmunoassay for TP revealed a crossreaction with a product found in spleen and lymph node. This product, named splenin, differs from TP only in position 34, aspartic acid for bovine TP and glutamic acid for bovine splenin and it was called TP III as well. Synthetic pentapeptides (TP-5) and (SP-5), reproduce the biological activities of TP and SP, respectively. It is now evident that various forms of TPs were created by proteolytic cleavage of larger proteins during isolation, cDNA clones have been isolated for three alternatively spliced mRNAs that encodes three distinct human T cell TPs. The immunomodulatory properties of TP, SP, TP-5, SP-5 and some of their synthetic analogs reported in the literature have been briefly reviewed.
Singh, V. K., Biswas, S., Mathur, K. B., Haq, W., Garg, S. K., & Agarwal, S. S. (1998). Thymopentin and splenopentin as immunomodulators. Immunologic research, 17(3), 345-368.
Splenopentin, Arg-Lys-Glu-Val-Tyr (SP-5) and its synthetic analogs; Arg-d-Lys-Glu-Val-Tyr (pentapeptide 1), Lys-Lys-Glu-Val-Tyr (2), d-Lys-Lys-Glu-Val-Tyr (3), Arg-Lys-Gly-Val-Tyr (4), and Arg-Lys-Gln-Val-Tyr (5) have been examined for augmentation of human natural killer (NK) cell activity and human T-cell transformation response. Pentapeptides 2 and 3 were found to significantly augment the in vitro human NK cell activity. However, none of them had any effect on lymphocyte proliferative responses.
Rastogi, A., Singh, V. K., Biswas, S., Haq, W., Mathur, K. B., & Agarwal, S. S. (1993). Augmentation of human natural killer cells by splenopentin analogs. FEBS letters, 317(1-2), 93-95.
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