Evidence Grade B — Strong clinical evidence. 1547 published studies, 398 human. 76 registered clinical trials.
Medically reviewed by a licensed medical professional
MGF (Mechano Growth Factor) is a 24-amino-acid peptide corresponding to a fragment of an IGF-1 variant that is naturally expressed in muscle after exercise or mechanical loading. No human clinical trials have been conducted. A fundamental question remains unresolved: whether this peptide fragment is actually produced and released as a standalone molecule in living tissue.
MGF (Mechano Growth Factor) is also known by these brand and alternate names:
1,547 published studies: 398 human, 388 animal, 217 in-vitro, 82 reviews
MGF has no marketing authorisation. No human clinical trials have been conducted. The evidence base consists of animal studies and cell culture experiments. A single mouse study reported increased muscle fibre size after intramuscular injection.
The compound's very short half-life (estimated minutes) in its native form has led to the development of PEGylated versions (PEG-MGF, #105) in unregulated channels, though this creates a pharmacologically distinct molecule. Products available through unregulated channels lack pharmaceutical quality assurance.
Research in animal models and cell culture suggests MGF may stimulate muscle precursor cell (satellite cell) proliferation through a mechanism that may be distinct from classical IGF-1 receptor signalling. These observations are from preclinical studies. The relationship between this isolated peptide fragment and the full-length IGF-1 splice variant's biological activity in intact human tissue is not established.
Research in animal models and cell cultures suggests MGF may stimulate muscle precursor cell growth, but the evidence base has significant caveats. Most research originates from a single laboratory, and a critical 2010 review stated there is inadequate evidence that this peptide is actually a product of natural gene expression — challenging the basic premise. The extremely short half-life (approximately 5-7 minutes) makes practical use challenging, which has led to PEGylated versions in unregulated channels. No human safety, dosing, or efficacy data exist from controlled trials. Products from unregulated sources lack pharmaceutical quality assurance.
PeptideTrace tracks 76 registered clinical trials for MGF (Mechano Growth Factor) sourced from ClinicalTrials.gov.
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MGF refers to the 24 amino acid C-terminal E-domain peptide (sequence: YQPPSTNKNTKSQRRKGSTFEEHK) derived from the IGF-1Ec splice variant in humans. Molecular weight is approximately 2,972 Da (C124H204N42O41S1). The IGF-1 gene produces multiple splice variants through alternative mRNA splicing; a 49 bp insert in exon 5 of the Ec variant creates a reading-frame shift producing this unique C-terminal sequence. The synthetic MGF peptide corresponds to these final 24 amino acids. It was first cloned from stretched muscle by Yang et al. (1996) in Geoffrey Goldspink's laboratory at University College London. The half-life is extremely short at approximately 5-7 minutes, and the peptide does not bind to known IGFBPs. Endogenous MGF mRNA expression increases within hours of mechanical muscle damage or exercise, preceding IGF-1Ea upregulation by days.
Research suggests MGF operates through a mechanism distinct from systemic IGF-1. Yang and Goldspink (2002) showed that MGF stimulates myoblast proliferation but suppresses differentiation, unlike IGF-1Ea, which promotes both. The prevailing hypothesis proposes a temporal signaling model: after muscle injury, IGF-1 gene splicing first favors the Ec/MGF variant to activate satellite cells, then shifts to Ea to promote differentiation and fusion. Research suggests MGF acts locally through autocrine/paracrine signaling, potentially involving PI3K/Akt and p38 MAPK pathways. Animal studies also suggest MGF upregulates superoxide dismutase activity and may have nuclear localization signals. The peptide appears to function independently of the IGF-1 receptor based on some research (Dluzniewska et al., 2005).
A single intramuscular injection of MGF in mice reportedly produced a 25% increase in mean muscle fiber size within 3 weeks. Dluzniewska et al. (2005) demonstrated neuroprotective effects in brain ischemia models functioning independently of the IGF-1 receptor. Carpenter et al. (2008) showed 35% less compromised cardiac muscle in sheep with induced myocardial infarction. Kandalla et al. (2011) found MGF increased proliferative lifespan of satellite cells from neonatal and young (but not old) human muscle progenitors. No clinical trials exist. No branded pharmaceutical product has been developed. The compound is not approved by any regulatory agency and is listed as a prohibited substance by WADA.
The information on this page is provided for educational and research reference purposes only. This is not medical advice. Always consult a qualified healthcare professional before making any health-related decisions.
Somatrogon is marketed as Ngenla (approved June 2023) for paediatric growth hormone deficiency in children aged 3 years and older. In the pivotal trial, once-weekly somatrogon produced growth rates equivalent to daily somatropin injections (10.1 cm/year versus 9.8 cm/year), confirming that reducing injection frequency does not compromise growth outcomes. Ngenla represents a meaningful advance for paediatric patients and their families, reducing injections from 365 to 52 per year. Treatment adherence has been a persistent challenge with daily growth hormone, and weekly dosing is expected to improve long-term outcomes through better compliance. Somatrogon competes directly with somapacitan (Sogroya), the other approved weekly growth hormone, creating a new generation of less burdensome treatment options.
Tesamorelin is marketed as Egrifta SV (approved November 2010) for the reduction of excess abdominal fat in HIV-infected patients with lipodystrophy. In clinical trials, it reduced visceral fat by approximately 15% compared to a 5% increase with placebo, and this reduction was sustained with continued treatment. Tesamorelin occupies a unique niche — it is the only approved GHRH analogue and the only medication specifically approved for HIV-associated lipodystrophy. Beyond its approved indication, it has attracted research interest for potential effects on liver fat, cognitive function, and peripheral neuropathy. Fat reduction reverses when treatment stops, and it is not approved for general weight loss or body composition purposes.
ACE-031 has no marketing authorisation. A Phase I trial in healthy women showed increased lean mass and decreased fat mass. A Phase II trial in DMD (24 patients) showed lean body mass increases but was discontinued due to bleeding-related safety concerns (epistaxis, telangiectasias, and gum bleeding), likely caused by inhibition of BMP-9/10 vascular signalling. ACE-031 is a large fusion protein (~90 kDa), not a peptide. Its clinical development was halted. The non-selective ligand-trapping profile — capturing beneficial vascular signalling molecules alongside the intended muscle-growth targets — illustrates the challenge of targeting the TGF-beta superfamily. Acceleron subsequently developed more selective agents.
This content is for informational purposes only and does not constitute medical advice. Always consult a qualified healthcare professional before making decisions about your health.
