MGF is a splice variant of the IGF-1 gene, called IGF-1Ec in humans. Resistance exercise raises its mRNA in the muscle of young men. No study has shown that an injected MGF peptide builds muscle, repairs tendon or does anything else in people, and no human trial of it exists.
The research splits in two. Several labs report that the 24-amino-acid E peptide drives muscle stem cells to multiply. Scientists at two pharmaceutical companies could not reproduce that. This page covers what MGF is, what each side found, where the evidence breaks down, and where MGF stands with FDA and WADA. It lists no doses. For the pegylated version, see our PEG-MGF page.
How to read it. Human biopsy: natural MGF mRNA, nothing given. Mouse or Animal data: peptide, plasmid or gene overexpression in animals. Cell data: dishes. None: no trial exists.
| Study | What was found | Peptide given to people? | Watch-out |
|---|---|---|---|
| Human | |||
| 1Damaging exercise in menBiopsy study | Human biopsyMGF mRNA rose rapidly and briefly, then IGF-1Ea and IGF-1Eb rose longer (1) | No | Natural mRNA. No peptide was given. |
| 2Lifting in young and older menBiopsy study | Human biopsyMGF mRNA rose 2.5 hours after leg exercise in young men, not in older men (2) | No | Natural mRNA. No peptide was given. |
| 3MGF peptide trialsClinical trials | NoneClinicalTrials.gov lists no MGF trial (3) | No | No human efficacy or safety data. |
| Animal | |||
| 4Mouse gene plasmidThe 25% figure | Mouse dataAn MGF gene plasmid raised fiber area 25% in 3 weeks (4) | No | The muscle made MGF itself. Cited to a patent. |
| 5Rat and rabbit muscleDamage and stretch | Animal dataMGF mRNA rose early after damage, then fell. Stretch raised both IGF-1 forms (5, 6) | No | mRNA only. |
| 6Mouse muscle bruiseMacrophage-depleted mice | Mouse dataMGF injection did not protect fiber regeneration. It reduced fibrosis (7) | No | One model, macrophages depleted. |
| 7Aging mouse brainNeurogenesis | Mouse dataGene overexpression from 1 or 3 months raised new neurons at 24 months, not from 12 months (8) | No | Gene overexpression, not a peptide. |
| 8Gerbil brainIschemia | Animal dataA synthetic peptide protected neurons (9) | No | One model. |
| 9Sheep and mouse heartHeart attack, function | Animal dataSheep: function preserved (10). Mice: peptides depressed function at 2 of 3 doses (11) | No | The two heart results conflict. |
| Cells | |||
| 10Muscle cells, first reportsProliferation, fusion | Cell dataRaised proliferation of mouse, pig and human muscle cells; the labs disagree on differentiation (12, 13, 14) | No | Human effect seen in young donors, not old (14). |
| 11Muscle cells, structureIGF1Ec parts | Cell dataThe N-terminal part promoted proliferation. The E sequence promoted differentiation and migration (15) | No | Contradicts the “blocks differentiation” idea. |
| 12Muscle cells, replicationTwo pharma labs | Cell dataNo effect up to 500 ng/mL in mouse, human and stem cells (16) | No | Questions a physiological role. |
| 13IGF-1 receptor assayReceptor activation | Cell dataThe MGF peptide and a stabilized analog did not activate the receptor (17) | No | Full-length MGF did, weaker than IGF-1. |
What is MGF?
MGF stands for mechano growth factor. The IGF-1 gene can be spliced into several forms. In humans, a 49-base insert shifts the reading frame and gives IGF-1Ec its own C-terminal tail, called the E domain (14). The mature IGF-1 region is identical in both forms (10). Researchers ascribed effects to a 24-amino-acid COOH-terminal peptide and named it MGF (16). That peptide is what labs synthesize and sellers list.
What happens to MGF in human muscle?
In one biopsy study, 10 men did exercise that damaged their muscle. Biopsies were taken before and at 6 hours, 2, 5 and 16 days. MGF mRNA rose rapidly and briefly. A longer rise in IGF-1Ea and IGF-1Eb mRNA followed. The protein patterns for MGF and IGF-1Ea were similar (1).
In another, 8 men aged 25 to 36 and 7 men aged 70 to 82 did 10 sets of 6 single-leg knee extensions at 80% of their one-repetition maximum. MGF mRNA rose 2.5 hours later in the young men but not in the older men. At rest, MGF mRNA was about 100 times lower than IGF-1Ea (2).
In rats, MGF mRNA rose first after muscle damage and fell within a few days, as IGF-1Ea rose (5). In rabbits, stretch raised both forms of IGF-1 mRNA (6). These studies measure the body’s own mRNA. They say nothing about injecting a peptide.
What does the case for the E peptide rest on?
The first report came from Goldspink’s group. The E domain raised myoblast proliferation and held back differentiation (12). Later cell studies agreed in part. In porcine satellite cells, MGF stimulated proliferation and inhibited differentiation. It also lowered MyoD, p21, myogenin and MEF2 expression (13).
In human muscle cells, the E peptide extended the proliferative life of neonatal and young adult cells but not older adult cells, and it increased fusion potential (14). In C2C12 cells, its proliferative effect was not blocked by an anti-IGF-1 receptor antibody and it did not phosphorylate Akt. That suggests a different route from mature IGF-1 (1).
The studies do not agree on differentiation. Yang and Qin reported inhibition, and Kandalla reported more fusion. A C2C12 structure-function study found that the N-terminal part of IGF1Ec promoted proliferation. The C-terminal E sequence promoted differentiation and migration (15).
What does the case against rest on?
Scientists at two pharmaceutical companies tried to reproduce it. Peptide concentrations up to 500 ng/mL did not raise the proliferation of mouse C2C12 cells or primary human myoblasts and did not block differentiation. Primary mouse muscle stem cells did not respond either. Mature IGF-1 and full-length IGF-1Eb did. They wrote that the results “call in to question whether there is a physiological role for MGF” (16).
A 2010 review found that no analogous peptide product of the Igf1 gene has been identified in cells, culture medium, tissues or body fluids (18). A 2016 receptor assay found that full-length MGF activated the IGF-1 receptor. Its EC50 was about nine times higher than IGF-1’s (7.83 against 0.86 nmol/L). The MGF peptide and a stabilized analog called Goldspink-MGF activated nothing (17).
Where does the 25% muscle growth figure come from?
It comes from Goldspink’s 2005 review. An MGF cDNA was put into a plasmid with muscle-specific regulatory sequences. After one injection into mouse muscle, mean fiber cross-sectional area rose 25% within three weeks. The review cites a US patent for the result, and a patent is not peer reviewed (4). The muscle made MGF itself from the gene, so the result says nothing about an injected peptide.
Does MGF help with aging?
The anti-aging argument comes mainly from Goldspink’s group. They argue that older muscle fails to raise MGF after exercise, which leaves the satellite cell pool unreplenished. They also report that growth hormone plus resistance exercise shifts IGF-1 splicing toward MGF and raises muscle cross-sectional area in elderly subjects (19). Those are review articles. The human work behind them is expression and biopsy data like the studies above.
The cell data cut the other way. The human E-peptide effect on proliferative life appeared in neonatal and young adult cells but not in older adult cells (14). In mice, brain MGF declines with age. Mice engineered to overexpress it from 1 or 3 months had more new neurons in the olfactory bulb at 24 months, but not when overexpression began at 12 months (8). That is gene overexpression. No peptide was given.
What have animal studies found?
In a gerbil model of brain ischemia, a synthetic MGF C-terminal peptide protected vulnerable neurons (9). In sheep after an induced heart attack, the MGF E domain preserved cardiac function and left 35% less compromised muscle (10). In mice, E-domain peptide variants depressed systolic and diastolic function at the lowest and highest of three doses over two weeks (11).
In mice with a muscle contusion and depleted macrophages, injecting MGF did not protect muscle fiber regeneration. It did reduce fibrosis and lowered inflammatory and matrix-metalloproteinase markers (7). We found no MGF peptide study in tendon, ligament or bone.
Is there any human evidence?
No. ClinicalTrials.gov lists no trial of MGF (3). The human data are biopsy studies of natural MGF mRNA. The exercise studies are often cited as human evidence for MGF peptides, but they measured gene expression after lifting or damage. Nothing in them involved giving a synthetic version.
MGF vs IGF-1
Mature IGF-1 is the same in both forms. In the replication study, every cell type responded to mature IGF-1 or full-length IGF-1Eb, and none responded to the MGF peptide (16).
MGF safety
No human safety study exists, so side effects are unknown. MGF comes from the IGF-1 gene, and higher circulating IGF-1 is associated with cancer risk. In UK Biobank (394,388 people), each 5 nmol/L higher IGF-1 went with higher risk of thyroid (HR 1.18), breast (1.11), prostate (1.08) and colorectal cancer (1.08), and lower risk of ovarian and liver cancer. Mean follow-up was 6.9 years, and the authors say reverse causality cannot be excluded (20).
That does not show that MGF raises cancer risk, because nobody has tested it. Goldspink’s group argues the peptide avoids the cancer concern attached to IGF-1 (14), but that is an argument and not a safety result. Anyone with a cancer history should talk to a clinician. The mouse heart result above is a caution about the class of peptides.
Is MGF legal, and is it banned in sport?
FDA has not approved MGF. Its 503A list places mechano growth factor in Category 3, nominated without adequate support (21). PEG-MGF sits on the nominated-but-withdrawn list with an immunogenicity warning (22). WADA’s 2026 Prohibited List names “Mechano growth factors (MGFs)” under S2, which is prohibited at all times (23). A “research use only” label is a seller’s wording and does not make human use legal.
How to judge an MGF listing
A certificate of analysis describes one lot. For a peptide it has to show identity as well as purity. Our peptide COA walkthrough goes through each step.
- Find a named lab you can search.
- Match the lot number on the vial to the report.
- Read the measured mass and compare it with the peptide the listing names.
- Look for an amount found, because purity alone does not give one.
Red flags are promised muscle gains, injection instructions on the product page, and a report for IGF-1 offered as proof of MGF. Our peptide vendor comparison covers sellers.
MGF questions
What is MGF peptide?
MGF, or mechano growth factor, is a splice variant of the IGF-1 gene. The peptide sold online is a synthetic 24-amino-acid fragment of its E domain. It is not an approved drug.
What does MGF do?
In cell and animal studies it has been reported to affect muscle cell growth, neurons and heart muscle. The results conflict, and no human trial exists.
Does MGF build muscle?
No study shows that an MGF peptide builds muscle in people. The 25% figure came from a mouse gene plasmid, not a peptide, and two pharmaceutical labs could not reproduce the cell result.
Can MGF help with aging or sarcopenia?
No trial shows it. The idea rests on reviews by the discoverer’s group, human expression data and cell studies. In one human cell study, the proliferation effect appeared in young donors but not older donors.
Has MGF been tested in humans?
Only as natural mRNA in muscle biopsies after exercise. ClinicalTrials.gov lists no trial of MGF.
Is MGF safe?
No human safety study exists. It comes from the IGF-1 gene, and higher IGF-1 is associated with some cancers in UK Biobank data, which cannot show that MGF itself carries that risk.
What is the difference between MGF and IGF-1?
They share the same mature region but have different E domains. In one replication study, cells responded to mature IGF-1 and not to the MGF peptide.
What is the difference between MGF and PEG-MGF?
PEG-MGF is MGF with polyethylene glycol attached. We found no published study of PEG-MGF itself. See our PEG-MGF page.
Is MGF banned in sport?
Yes. WADA’s 2026 Prohibited List names mechano growth factors under S2, prohibited at all times.
MGF is a research chemical for laboratory use only. It is not approved by FDA as a drug or dietary supplement and is not intended to diagnose, treat, cure or prevent any disease.
Show references (23)Hide references
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- Hameed M, Orrell RW, Cobbold M, Goldspink G, Harridge SD. Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise. J Physiol. 2003;547(Pt 1):247-254. PMID 12562960.
- ClinicalTrials.gov. Search results for mechano growth factor.
- Goldspink G. Mechanical signals, IGF-I gene splicing, and muscle adaptation. Physiology (Bethesda). 2005;20:232-238. PMID 16024511.
- Hill M, Goldspink G. Expression and splicing of the insulin-like growth factor gene in rodent muscle is associated with muscle satellite (stem) cell activation following local tissue damage. J Physiol. 2003;549(Pt 2):409-418. PMID 12692175.
- McKoy G, Ashley W, Mander J, et al. Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation. J Physiol. 1999;516(Pt 2):583-592. PMID 10087355.
- Liu X, Zeng Z, Zhao L, Chen P, Xiao W. Impaired skeletal muscle regeneration induced by macrophage depletion could be partly ameliorated by MGF injection. Front Physiol. 2019;10:601. PMID 31164836.
- Tang JJ, Podratz JL, Lange M, Scrable HJ, Jang MH, Windebank AJ. Mechano growth factor, a splice variant of IGF-1, promotes neurogenesis in the aging mouse brain. Mol Brain. 2017;10(1):23. PMID 28683812.
- Dluzniewska J, Sarnowska A, Beresewicz M, et al. A strong neuroprotective effect of the autonomous C-terminal peptide of IGF-1 Ec (MGF) in brain ischemia. FASEB J. 2005;19(13):1896-1898. PMID 16144956.
- Carpenter V, Matthews K, Devlin G, et al. Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Heart Lung Circ. 2008;17(1):33-39. PMID 17581790.
- Solís C, Thompson WC, Peña JR, et al. Mechano-growth factor E-domain modulates cardiac contractile function through 14-3-3 protein interactomes. Front Physiol. 2022;13:1028345. PMID 36467694.
- Yang SY, Goldspink G. Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett. 2002;522(1-3):156-160. PMID 12095637.
- Qin L, Li X, Xu J, et al. Mechano growth factor (MGF) promotes proliferation and inhibits differentiation of porcine satellite cells (PSCs) by down-regulation of key myogenic transcriptional factors. Mol Cell Biochem. 2012;370(1-2):221-230. PMID 22875667.
- Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. 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. Mech Ageing Dev. 2011;132(4):154-162. PMID 21354439.
- Yi Q, Feng J, He L, et al. The structure-function relationships of insulin-like growth factor 1 Ec in C2C12 cells. Cell Adh Migr. 2018;12(1):47-55. PMID 28471324.
- Fornaro M, Hinken AC, Needle S, et al. 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. Am J Physiol Endocrinol Metab. 2014;306(2):E150-E156. PMID 24253050.
- Janssen JA, Hofland LJ, Strasburger CJ, van den Dungen ES, Thevis M. Potency of full-length MGF to induce maximal activation of the IGF-I R is similar to recombinant human IGF-I at high equimolar concentrations. PLoS One. 2016;11(3):e0150453. PMID 26991004.
- Matheny RW, Nindl BC, Adamo ML. Minireview: mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology. 2010;151(3):865-875. PMID 20130113.
- Goldspink G. Age-related muscle loss and progressive dysfunction in mechanosensitive growth factor signaling. Ann N Y Acad Sci. 2004;1019:294-298. PMID 15247032.
- Knuppel A, Fensom GK, Watts EL, et al. Circulating insulin-like growth factor-I concentrations and risk of 30 cancers: prospective analyses in UK Biobank. Cancer Res. 2020;80(18):4014-4021. PMID 32709735.
- FDA. Bulk drug substances nominated for use in compounding under section 503A of the FD&C Act. Category 3 list, updated May 14, 2026.
- FDA. Certain bulk drug substances for use in compounding that may present significant safety risks.
- World Anti-Doping Agency. 2026 Prohibited List, class S2 (copy hosted by the Dutch government).
