PEG-MGF Product Description
Alternative splicing of the IGF-1 gene produces several E-domain variants. The IGF-1Ec transcript carries an insert that shifts the reading frame at the 3′ end, and the final 24 residues of that E-domain are the sequence studied under the research designation Mechano Growth Factor.
The synthetic 24-residue peptide has been examined as a distinct entity from mature IGF-1, and the two behave differently in culture. Reviews of the literature note that no analogous peptide product of the Igf1 gene has been isolated from cultured cells or conditioned medium, so the material used in research is synthetic.
PEG-MGF applies a peptide modification step to that base sequence. The polyethylene glycol conjugate raises hydrodynamic radius and slows proteolytic clearance in solution, which is why PEGylated analogs are used where the unmodified sequence is short-lived. The material ships freeze-dried.
Compound Specifications
Note for laboratories: Identifier values below describe the base MGF (24-residue) peptide unless the row states otherwise. The PEGylated form has no single canonical registry entry because molecular weight varies with PEG chain length and attachment chemistry.
| Property |
Value |
| Compound Class |
PEGylated synthetic peptide, IGF-1Ec E-domain C-terminal fragment |
| CAS Number (PEG-MGF) |
[verify] no registry-verified CAS located for the PEGylated form |
| PubChem CID (base MGF peptide) |
175675731 |
| Molecular Formula (base MGF peptide) |
C₁₂₁H₁₉₉N₄₁O₄₀ |
| Molecular Weight (base MGF peptide) |
2868.1 g/mol |
| Monoisotopic Mass (base MGF peptide) |
2866.4798 Da |
| InChIKey (base MGF peptide) |
TXMSCWQMYNJNDC-XGJLPCLZSA-N |
| Amino Acid Sequence (one-letter) |
YQPPSTNKNTKSQRRKGSTFEERK |
| Amino Acid Sequence (three-letter) |
Tyr-Gln-Pro-Pro-Ser-Thr-Asn-Lys-Asn-Thr-Lys-Ser-Gln-Arg-Arg-Lys-Gly-Ser-Thr-Phe-Glu-Glu-Arg-Lys |
| Sequence Length |
24 residues |
| Source |
Synthetic, solid-phase peptide synthesis followed by PEG conjugation |
| Purity |
≥99% (HPLC) |
| Appearance |
Lyophilized white powder |
| Solubility |
Soluble in water and in bacteriostatic water |
| Storage |
-20°C, protect from light |
| Vial Size |
5mg |
Storage and Handling
- Store the lyophilized compound at -20°C, protected from light.
- After reconstitution, store at 2°C to 8°C and use promptly.
- Maintain aseptic handling 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.
PEG MGF Research
The published literature on this sequence concerns the unmodified 24-residue MGF peptide. Work on the PEGylated analog is not indexed in PubMed, so the observations below describe the base peptide in laboratory models.
In primary skeletal myoblast cultures isolated from donors of different ages, the synthetic MGF 24-residue E peptide was associated with an extended proliferative life span and delayed senescence in neonatal and young adult cultures, but not in cultures from older adult tissue [2]. Investigators studying porcine satellite cells reported increased proliferation alongside reduced transcript levels of MyoD, p21, myogenin, and MEF2A [3].
Structure-function work in C2C12 murine myoblasts separated the two halves of IGF-1Ec. The N-terminal region tracked with proliferation, while the C-terminal region identical to the MGF E sequence tracked with differentiation and migration readouts [4]. Comparable sequence-level questions come up in other myogenic signaling research, including work on follistatin.
Migration is the most consistently reported observation across these models, so several groups have looked at the pathways behind it.
Migration and Receptor Pathway Studies
In myogenic precursor cell cultures, the MGF C-terminal 24-residue peptide was associated with raised expression of u-PA, u-PAR, and MMP-7 and reduced PAI-1 activity, with no change in MMP-2 or MMP-9, through a mechanism the authors reported as independent of the IGF-1 receptor [5]. In rat bone marrow stromal cell cultures, the same peptide showed no proliferative change but raised migration in scratch and transwell migration assays, with the migration response blocked by either Erk1/2 inhibition or IGF-1 receptor blockade [6].
The literature is not uniform. A replication attempt run across two pharmaceutical laboratories found no proliferative change in C2C12 cells or primary skeletal myoblast cultures at peptide concentrations up to 500 ng/ml, and no p-ERK activation in cardiac myocytes [7]. That contrast is one reason the sequence remains an active in vitro research subject, and it is also why the serum stability period of the peptide, addressed here through PEGylation, is relevant to experimental design alongside general peptide stability and storage practice.
| Research Area |
In Vitro Application |
| Myoblast Proliferation Signaling |
Proliferation and senescence readouts in C2C12 and primary skeletal myoblast cultures |
| Satellite Cell Transcriptional Profiling |
Porcine satellite cell models measuring MyoD, myogenin, p21, and MEF2A transcript levels |
| Cell Migration Assays |
Scratch and transwell migration assays in myogenic precursor and bone marrow stromal cell cultures |
| Receptor and Pathway Mapping |
Erk1/2 phosphorylation and IGF-1 receptor dependence studies |
| Peptide Modification Chemistry |
Comparative analysis of PEGylated and unmodified sequence serum stability period |
References
- Matheny RW, Nindl BC, Adamo ML (2010). Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology. https://pmc.ncbi.nlm.nih.gov/articles/PMC2840678/
- Kandalla PK, Goldspink G, Butler-Browne G, Mouly V (2011). Mechano Growth Factor E peptide (MGF-E), derived from an isoform of IGF-1, activates human muscle progenitor cells and induces an increase in their fusion potential at different ages. Mechanisms of Ageing and Development. https://www.sciencedirect.com/science/article/abs/pii/S0047637411000297
- Qin LL, Li XK, Xu J, et al. (2012). Mechano growth factor (MGF) promotes proliferation and inhibits differentiation of porcine satellite cells (PSCs) by down-regulation of key myogenic transcriptional factors. Molecular and Cellular Biochemistry. https://link.springer.com/article/10.1007/s11010-012-1413-9
- Yi Q, Feng J, He L, et al. (2017). The structure-function relationships of insulin-like growth factor 1 Ec in C2C12 cells. Cell Adhesion & Migration. https://pmc.ncbi.nlm.nih.gov/articles/PMC5810762/
- Mills P, Lafrenière JF, Benabdallah BF, El Fahime EM, Tremblay JP (2007). A new pro-migratory activity on human myogenic precursor cells for a synthetic peptide within the E domain of the mechano growth factor. Experimental Cell Research. https://doi.org/10.1016/j.yexcr.2006.10.032
- Cui H, Yi Q, Feng J, Yang L, Tang L (2014). Mechano growth factor E peptide regulates migration and differentiation of bone marrow mesenchymal stem cells. Journal of Molecular Endocrinology. https://jme.bioscientifica.com/view/journals/jme/52/2/111.xml
- Fornaro M, Hinken AC, Needle S, et al. (2014). Mechano-growth factor peptide, the COOH terminus of unprocessed insulin-like growth factor 1, has no apparent effect on myoblasts or primary muscle stem cells. American Journal of Physiology-Endocrinology and Metabolism. https://journals.physiology.org/doi/full/10.1152/ajpendo.00408.2013
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PEG-MGF (260699)
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