Pancragen Product Description
Pancragen is a four-residue peptide built from lysine, glutamic acid, aspartic acid, and tryptophan. Its low molecular weight and charge distribution place it in the class of short regulatory peptides that have been examined for nuclear localization and direct interaction with chromatin.
The compound is one of several tissue-designated short peptides developed at the Saint Petersburg Institute of Bioregulation and Gerontology. Within that series, KEDW is the sequence associated with pancreatic tissue research models, while related sequences such as AEDL and AEDG are associated with other tissue types.
Laboratory interest in Pancragen centers on two research threads. The first is its interaction with DNA and histone proteins at defined nucleotide motifs. The second is the pattern of differentiation-marker expression observed in cultured pancreatic cells exposed to the peptide.
Compound Specifications
| Property |
Value |
| PubChem CID |
68452877 |
| Molecular Formula |
C₂₆H₃₆N₆O₉ |
| Molecular Weight |
576.60 g/mol |
| Monoisotopic Mass |
576.25438 Da |
| Amino Acid Sequence |
H-Lys-Glu-Asp-Trp-OH (KEDW) |
| Sequence Length |
4 residues |
| IUPAC Name |
(4S)-5-[[(2S)-3-carboxy-1-[[(1S)-1-carboxy-2-(1H-indol-3-yl)ethyl]amino]-1-oxopropan-2-yl]amino]-4-[[(2S)-2,6-diaminohexanoyl]amino]-5-oxopentanoic acid |
| InChIKey |
PIGJHNNSOMRLST-LEAZDLGRSA-N |
| Canonical SMILES |
C1=CC=C2C(=C1)C(=CN2)CC(C(=O)O)NC(=O)C(CC(=O)O)NC(=O)C(CCC(=O)O)NC(=O)C(CCCCN)N |
| Source |
Synthetic |
| Related Amide Form |
H-Lys-Glu-Asp-Trp-NH₂ (PubChem CID 68451868, C₂₆H₃₇N₇O₈, 575.6 g/mol) |
| Purity |
≥99% (HPLC) |
| Appearance |
Lyophilized white powder |
| Solubility |
Soluble in water; sterile bacteriostatic water is commonly used for reconstitution |
| Storage |
-20°C, protect from light |
Storage and Handling
- Store the lyophilized compound at -20°C, protected from light and moisture.
- After reconstitution, store at 2°C to 8°C and use promptly; for extended holding, aliquot and store at -20°C to limit freeze-thaw cycles.
- Allow the sealed vial to equilibrate to room temperature before opening to reduce condensation on the powder.
- Maintain aseptic handling throughout to preserve compound integrity.
Lyophilized Format
This compound ships in lyophilized (freeze-dried) form. Freeze-drying supports long-term storage stability and preserves compound integrity. No fillers are added.
Pancragen Research
Molecular modeling work on short peptides places KEDW among sequences that bind DNA at defined nucleotide motifs. Docking studies assign KEDW and AED to the acct binding site, with binding specificity tracking the primary sequence of both the peptide and the target oligonucleotide [1].
Follow-up molecular mechanics work examined how the tetrapeptide approaches the DNA duplex. The analysis reported interaction with both the minor and the major groove, with major-groove contact showing greater sequence dependence and GGCAG identified as a putative binding site [2].
A separate line of work looked at peptide binding to histone proteins. Using fluorescence quenching with FITC-labeled wheat histones, KEDW was among the short peptides observed to bind at N-terminal histone regions, with binding modulated by the presence and methylation state of associated oligonucleotides [3]. This chromatin-level interaction is one of the proposed routes by which short peptide bioregulators are thought to reach gene expression.
The pancreatic-tissue research thread runs through cell culture models rather than modeling alone.
Differentiation-Marker Expression in Pancreatic Cell Cultures
In cultured pancreatic cells, expression of differentiation markers was reported to decline across passage number. Exposure to the KEDW tetrapeptide was associated with increased expression of acinar markers Pdx1 and Ptf1a and islet markers Pdx1, Pax6, Pax4, Foxa2, and Nkx2.2 in both early-passage and late-passage cultures [4].
Tissue specificity is a recurring observation in this series. In parallel cultures, KEDW was associated with changes in CXCL12 and Hoxa3 expression in pancreatic cells, while the AEDL sequence acted on bronchial epithelial cells and KED on fibroblasts, with each peptide showing its effect in its designated tissue culture rather than across all three [5].
Promoter Methylation and Epigenetic Framing
Work on DNA methylation examined whether promoter state accompanies these expression changes. Methylation patterns at the PDX1, PAX6, and NGN3 promoter regions shifted across culture age in correlation with expression level, and KEDW was associated with changes in methylation at the FOXA2 promoter region [6]. Other promoters in the same panel, including PAX4, showed expression changes without a matching methylation shift, indicating more than one mechanism is in play.
Reviews of the short peptide series place KEDW alongside AEDL as sequences associated with directed differentiation toward pancreatic and lung cell lineages respectively [7]. More recent work in tissue engineering has included KEDW in surveys of short peptides examined for their capacity to influence stem cell fate toward pancreatic lineages in scaffold and matrix contexts [8].
| Research Area |
In Vitro Application |
| Peptide-DNA interaction |
Docking and molecular mechanics studies of sequence-specific binding at defined nucleotide motifs |
| Chromatin and histone binding |
Fluorescence-based assays of peptide association with histone N-terminal regions |
| Pancreatic cell differentiation |
Expression profiling of Pdx1, Pax4, Pax6, Foxa2, and Nkx2.2 in cultured pancreatic cells |
| Epigenetic regulation |
Promoter methylation analysis across culture passage number |
| Cellular aging models |
Comparison of marker expression between early-passage and late-passage cultures |
| Stem cell fate research |
Short peptide screening in scaffold and matrix systems for lineage direction |
References
- Khavinson VK, Lin’kova NS, Tarnovskaya SI (2016). Short Peptides Regulate Gene Expression. Bulletin of Experimental Biology and Medicine, 162(2), 288-292. https://doi.org/10.1007/s10517-016-3596-7
- Tarnovskaya SI, Yakutseni PP, Khavinson VK (2014). Study of interactions between DNA and tetrapeptides using methods of molecular mechanics. Bulletin of Experimental Biology and Medicine, 156(5), 689-693. https://doi.org/10.1007/s10517-014-2426-z
- Fedoreyeva LI, Smirnova TA, Kolomijtseva GY, Khavinson VK, Vanyushin BF (2013). Interaction of short peptides with FITC-labeled wheat histones and their complexes with deoxyribooligonucleotides. Biochemistry (Moscow), 78(2), 166-175. https://doi.org/10.1134/S0006297913020053
- Khavinson VK, Durnova AO, Polyakova VO, Tolibova GH, Linkova NS, Kvetnoy IM, Kvetnaia TV, Tarnovskaya SI (2013). Effects of pancragen on the differentiation of pancreatic cells during their ageing. Bulletin of Experimental Biology and Medicine, 154(4), 501-504. https://doi.org/10.1007/s10517-013-1987-6
- Khavinson VK, Linkova NS, Polyakova VO, Kheifets OV, Tarnovskaya SI, Kvetnoy IM (2012). Peptides tissue-specifically stimulate cell differentiation during their aging. Bulletin of Experimental Biology and Medicine, 153(1), 148-151. https://doi.org/10.1007/s10517-012-1664-1
- Ashapkin VV, Linkova NS, Khavinson VK, Vanyushin BF (2015). Epigenetic mechanisms of peptidergic regulation of gene expression during aging of human cells. Biochemistry (Moscow), 80(3), 310-322. https://doi.org/10.1134/S0006297915030062
- Khavinson V, Linkova N, Diatlova A, Trofimova S (2020). Peptide Regulation of Cell Differentiation. Stem Cell Reviews and Reports, 16(1), 118-125. https://doi.org/10.1007/s12015-019-09938-8
- Vishwanath R, Biswas A, Modi U, Gupta S, Bhatia D, Solanki R (2025). Programmable short peptides for modulating stem cell fate in tissue engineering and regenerative medicine. Journal of Materials Chemistry B, 13(8), 2573-2591. https://doi.org/10.1039/d4tb02102a
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Endotoxin Pancragen
Pancragen 20 mg (11358)
Pancragen (251519)
Pancragen (251519E)
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