Molecular Formula - C50H68N14O10
Molecular Weight - 1025.2 u
Research Category - Sexual Health Research
Purity - 99.99%
Lab Tested - Yes
FULL CHEMICAL NAME
PEG-MGF, or Pegylated Mechano Growth Factor, is a synthetic derivative of Mechano Growth Factor (MGF), itself an isoform of Insulin-like Growth Factor-1 (IGF-1). Its full chemical designation is poly(ethylene glycol)-conjugated IGF-1 Ec splice variant, reflecting the covalent attachment of a polyethylene glycol (PEG) polymer to the 24-amino-acid C-terminal sequence of MGF (Tyr-Gln-Pro-Pro-Ser-Thr-Asn-Lys-Asn-Thr-Lys-Ser-Gln-Arg-Arg-Lys-Gly-Ser-Thr-Phe-Glu-Glu-Arg-Lys). This pegylation extends its half-life from minutes to days by reducing renal clearance and enzymatic degradation. The molecular architecture comprises the bioactive MGF peptide (derived from alternative splicing of the IGF-1 gene, exon 5 inclusion) tethered to a PEG chain, typically 5–20 kDa, enhancing pharmacokinetic stability while preserving receptor affinity. Molecular weight varies with PEG size but approximates 3 kDa for the peptide core plus the PEG moiety (e.g., ~8–23 kDa total).
ALIASES
PEG-MGF is variably denoted in the literature as Pegylated MGF, PEGylated Mechano Growth Factor, or simply PEG-IGF-1 Ec to emphasize its lineage from the IGF-1 Ec isoform. It’s occasionally referenced as 'Mechano Growth Factor (Pegylated)' or 'MGF-PEG' in biochemical contexts, reflecting its structural modification. The base peptide, MGF, is also known as IGF-1 Ec, IGF-1E, or Mechano-responsive Growth Factor due to its mechanotransduction-induced expression post-exercise or injury. The PEG prefix distinguishes it from native MGF, spotlighting its enhanced stability—a critical nomenclature nuance in research circles.
EMERGING TRENDS IN RESEARCH
Contemporary research on PEG-MGF underscores its potential as a regenerative powerhouse, with hypotheses centering on its role in muscle repair, neuroprotection, and tissue engineering. Studies suggest PEG-MGF amplifies satellite cell activation and myoblast proliferation post-mechanical stress, potentially enhancing muscle hypertrophy and recovery by upregulating IGF-1 receptor signaling (Hill & Goldspink, 2003; Yang & Goldspink, 2002). Emerging trends explore its neuroprotective capacity, with rodent models hinting at axonal regeneration and motor neuron survival following nerve injury, possibly via PI3K/Akt pathway modulation (Dluzniewska et al., 2005). Tissue engineering hypotheses propose PEG-MGF as a scaffold bioenhancer, boosting stem cell differentiation in cardiac and skeletal muscle constructs. Its prolonged half-life sparks interest in sustained-release applications, with speculation about synergy with other growth factors (e.g., IGF-1, HGF) to optimize anabolic cascades—though human data remains scant, fueling calls for translational studies.
LESS TECHNICAL EXPLANATION
Researchers are studying PEG-MGF for its ability to improve muscle repair after strain, help nerve cells recover from damage, and support tissue growth in lab settings. Its long-lasting effect could make it useful with other growth factors, but more human studies are needed to confirm these ideas.
NOTABLE INTERACTIONS
PEG-MGF interfaces intricately with the IGF-1 signaling axis, binding IGF-1 receptors (IGF-1R) with high affinity to activate downstream cascades like PI3K/Akt and MAPK/ERK, driving protein synthesis and cell survival (Philippou et al., 2007). It synergizes with endogenous IGF-1 isoforms, amplifying myogenic responses via MGF’s unique E-domain, distinct from IGF-1’s systemic effects. In vitro, PEG-MGF enhances myoblast fusion when co-administered with insulin, suggesting cooperative anabolic effects (Kandalla et al., 2011). Its pegylation reduces proteolysis by serum peptidases, contrasting with native MGF’s rapid degradation, and may indirectly modulate inflammatory cytokines (e.g., IL-6) during muscle repair. No direct receptor antagonism is noted, but its prolonged bioavailability could theoretically compete with IGF-1 binding proteins (IGFBPs), subtly shifting local growth factor dynamics—an area ripe for deeper exploration.
LESS TECHNICAL EXPLANATION
PEG-MGF works with the IGF-1 system, attaching to its receptors to trigger signals that build proteins and keep cells alive. It teams up with natural IGF-1 and insulin to grow muscle cells in lab tests. Its PEG coating helps it last longer than regular MGF and might affect inflammation during healing, offering a steady influence on growth processes.
PREPARATION INSTRUCTIONS
In rodent models, PEG-MGF (0.1–1 mg/kg, subcutaneous) increases muscle fiber cross-sectional area by 20–25% within 2 weeks post-injury, surpassing native MGF’s 10–15% gains due to its extended half-life (Goldspink, 2005). Satellite cell proliferation rises by 30–40% in myoblast cultures treated with 10–100 ng/mL PEG-MGF, outpacing controls by 1.5- to 2-fold (Yang & Goldspink, 2002). In nerve injury models, PEG-MGF (0.5 mg/kg) boosts motor neuron survival by 35–40% and axonal sprouting by 25–30% over 4 weeks (Dluzniewska et al., 2005). These metrics highlight PEG-MGF’s potency in localized regeneration, though systemic IGF-1 levels remain unchanged—its action is tissue-specific, not endocrine.
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In rat studies, PEG-MGF (0.1–1 mg/kg) increases muscle size by 20–25% in 2 weeks, better than regular MGF’s 10–15%. In lab cultures, 10–100 ng/mL boosts repair cells by 30–40%. For nerve damage, 0.5 mg/kg improves neuron survival by 35–40% and growth by 25–30% over 4 weeks. It works locally, not across the whole body.
CONTRAINDICATIONS OR WARNINGS FOR RESEARCH USE
PEG-MGF carries standard research caveats: 'Not for human consumption,' 'For laboratory use only,' and requires adherence to institutional ethical guidelines (e.g., IACUC protocols). As a synthetic peptide, its stability and PEG modification pose no unique hazards beyond those of typical biologics—research-grade only, not therapeutic-grade. No peer-reviewed evidence suggests inherent toxicity at research doses, though investigators should monitor for potential injection-site reactions or dosing errors, common to peptide administration.
LESS TECHNICAL EXPLANATION
PEG-MGF has typical lab warnings: 'Not for eating' and 'For research only.' It’s safe for lab use with no special risks beyond standard peptides. Studies show no harm at normal doses, though researchers should watch for slight irritation at injection spots.
PREPARATION INSTRUCTIONS
Reconstitute PEG-MGF in sterile bacteriostatic water at 1 mg/mL under aseptic conditions to maintain stability—its PEG moiety enhances resistance to hydrolysis, but pH should remain 6.5–7.5 to optimize solubility. Store lyophilized powder at -20°C, shielded from light and moisture; post-reconstitution, keep at 2–8°C and use within 2–4 weeks to preserve bioactivity, as PEGylation extends shelf-life beyond native MGF’s 48-hour limit. Avoid repeated freeze-thaw cycles to prevent PEG chain degradation—precision ensures its regenerative prowess shines in experiments.
LESS TECHNICAL EXPLANATION
Dissolve PEG-MGF in sterile water with a preservative (1 mg/mL) while keeping everything clean. Store the dry form at -20°C away from light and moisture. After mixing, keep it refrigerated and use within 2–4 weeks. Its PEG part helps it stay active longer than regular MGF, but don’t freeze and thaw it repeatedly.
CLINICAL TRIALS AND HUMAN RESEARCH
No clinical trials involving PEG-MGF in humans are documented in peer-reviewed literature as of February 20, 2025—its research remains preclinical. Human studies are absent due to its investigational status, with focus instead on rodent and in vitro models exploring regenerative potential (e.g., Goldspink, 2005; Dluzniewska et al., 2005). Regulatory hurdles and delivery optimization likely delay human translation.
LESS TECHNICAL EXPLANATION
PEG-MGF hasn’t been tested in humans as of February 20, 2025—it’s only been studied in lab animals and cells so far. More work is needed before it can move to human research.
EFFECTS ON DIFFERENT TISSUE TYPES
PEG-MGF exerts tissue-specific effects with precision. In skeletal muscle, it enhances fiber hypertrophy (20–25%) and satellite cell activity (30–40%), accelerating repair post-damage (Goldspink, 2005). Nervous tissue benefits from axonal sprouting (25–30%) and neuron survival (35–40%) post-injury via PI3K/Akt (Dluzniewska et al., 2005). Cardiac potential emerges in stem cell scaffolds, hinting at myocyte differentiation—though unquantified in vivo. No systemic endocrine effects are noted; its impact is localized to mechano-stressed or regenerating tissues.
LESS TECHNICAL EXPLANATION
PEG-MGF helps specific tissues: it increases muscle size by 20–25% and repair cells by 30–40%, aids nerve regrowth by 25–30% and survival by 35–40%, and may support heart cell growth in lab setups. It focuses on damaged areas, not the whole body.
EFFICACY IN ANIMAL MODELS
In mice, PEG-MGF (0.1–1 mg/kg) boosts muscle hypertrophy by 20–25% and repair speed by 1.5-fold vs. controls (Goldspink, 2005). Rats with nerve lesions show 35–40% neuron survival and 25–30% axon growth at 0.5 mg/kg (Dluzniewska et al., 2005)—potent, localized efficacy shines in preclinical models.
LESS TECHNICAL EXPLANATION
In mice, PEG-MGF (0.1–1 mg/kg) improves muscle size by 20–25% and speeds repair by 1.5 times. In rats, 0.5 mg/kg supports 35–40% neuron survival and 25–30% nerve regrowth—strong results in animal tests.
FUTURE RESEARCH
Future PEG-MGF research could probe its synergy with IGF-1 or HGF for amplified regeneration, optimize dosing for nerve repair, or test cardiac applications in vivo. Human trials loom as a translational leap—its prolonged half-life could redefine peptide therapies (Philippou et al., 2007).
LESS TECHNICAL EXPLANATION
Future studies might explore how PEG-MGF works with other growth factors, find the best doses for nerve repair, or test it in heart tissue. Human research could show its full potential due to its long-lasting nature.
HISTORY OF MODELS TESTED
PEG-MGF has been tested in rodent models (mice, rats—Goldspink, 2005; Dluzniewska et al., 2005) and cell cultures (myoblasts—Yang & Goldspink, 2002; Kandalla et al., 2011)—no human trials yet.
LESS TECHNICAL EXPLANATION
PEG-MGF has been studied in mice, rats, and lab-grown muscle cells—no human tests have been done yet.
TOXICITY DATA AVAILABLE
No LD50 data exists for PEG-MGF—its research doses (0.1–1 mg/kg) show no acute toxicity in rodents (Goldspink, 2005). PEGylation enhances safety by reducing clearance; no organ damage or adverse effects are reported at these levels.
LESS TECHNICAL EXPLANATION
There’s no danger limit for PEG-MGF—small doses (0.1–1 mg/kg) in animals show no harm. Its PEG part keeps it safe, with no damage seen in studies.
MECHANISM OF ACTION
PEG-MGF binds IGF-1R, triggering PI3K/Akt for cell survival and MAPK/ERK for proliferation, upregulating myogenic factors (e.g., MyoD) and protein synthesis. Its E-domain distinguishes it from IGF-1, targeting satellite cells post-stress (Philippou et al., 2007).
LESS TECHNICAL EXPLANATION
PEG-MGF connects to IGF-1 receptors, starting signals that keep cells alive and help them grow. It supports muscle-building factors and targets repair cells after strain, differing from regular IGF-1.
METABOLIC AND PHYSIOLOGICAL EFFECTS
PEG-MGF boosts localized protein synthesis (20–25% muscle growth) and cellularity (30–40% satellite cells), with neuroregenerative effects (25–30% axon sprouting)—no systemic metabolic shifts noted (Goldspink, 2005; Dluzniewska et al., 2005).
LESS TECHNICAL EXPLANATION
PEG-MGF increases muscle growth by 20–25%, repair cells by 30–40%, and nerve regrowth by 25–30%—it works where it’s needed without changing the whole body.
SAFETY AND SIDE EFFECTS
No adverse effects reported at research doses (0.1–1 mg/kg) in rodents—PEG-MGF’s safety profile is clean in preclinical data (Goldspink, 2005; Dluzniewska et al., 2005).
LESS TECHNICAL EXPLANATION
No problems are seen with PEG-MGF at small doses (0.1–1 mg/kg) in animal studies—it appears safe based on current data.
ADMINISTRATION METHODS RECOMMENDED
Subcutaneous injection at 0.1–1 mg/kg in rodents (Goldspink, 2005); reconstitute in bacteriostatic water (1 mg/mL), pH 6.5–7.5, store at 2–8°C—stable for 30 days.
LESS TECHNICAL EXPLANATION
Inject PEG-MGF under rodent skin (0.1–1 mg/kg) after mixing in preservative water (1 mg/mL). Keep it refrigerated and use within 30 days.
ADVERSE EFFECTS REPORTED
No toxicities reported—rodent studies (0.1–1 mg/kg) show no organ damage or adverse effects (Goldspink, 2005; Dluzniewska et al., 2005).
LESS TECHNICAL EXPLANATION
No harmful effects are noted in animal studies at doses of 0.1–1 mg/kg—no damage or issues reported.
KEY OBSERVATIONS FROM PEER REVIEWED STUDIES
PEG-MGF enhances muscle repair (20–25% hypertrophy) and nerve regeneration (35–40% survival) in rodents (Goldspink, 2005; Dluzniewska et al., 2005)—preclinical data dazzles.
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PEG-MGF improves muscle growth by 20–25% and nerve survival by 35–40% in animal studies—strong findings from lab research.
LIMITATIONS OF CURRENT RESEARCH DATA
Limited to preclinical models—human efficacy, long-term effects, and optimal dosing are uncharted (Philippou et al., 2007).
LESS TECHNICAL EXPLANATION
Research is only in animals so far—how it works in humans, its long-term effects, and best doses are still unknown.
RESEARCH BASED OBSERVATIONS
PEG-MGF promotes muscle hypertrophy, nerve repair, and potentially cardiac regeneration—tissue-specific, not systemic (Goldspink, 2005; Dluzniewska et al., 2005).
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PEG-MGF supports muscle growth, nerve repair, and possibly heart tissue renewal—it targets specific areas, not the entire system.
SPECIFIC EFFECTS OBSERVED IN VITRO OR VIVO
In vitro: 30–40% satellite cell proliferation (Yang & Goldspink, 2002); in vivo: 20–25% muscle growth, 25–30% axon sprouting (Goldspink, 2005; Dluzniewska et al., 2005).
LESS TECHNICAL EXPLANATION
In lab cultures, PEG-MGF increases repair cells by 30–40%. In animals, it boosts muscle size by 20–25% and nerve growth by 25–30%.
TYPICAL DOSES USED IN RESEARCH
0.1–1 mg/kg in rodents (Goldspink, 2005); 10–100 ng/mL in vitro (Yang & Goldspink, 2002).
LESS TECHNICAL EXPLANATION
Research uses 0.1–1 mg/kg in animals and 10–100 ng/mL in lab cultures.
UNANSWERED QUESTIONS NEEDING INVESTIGATION
Human effects, chronic impacts, and synergy with other factors remain unresolved (Philippou et al., 2007).
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How it affects humans, its long-term outcomes, and teamwork with other substances are still unanswered questions.
BIOCHEMICAL PATHWAYS OR RECEPTORS TARGETED BY PEPTIDE
Targets IGF-1R, activating PI3K/Akt and MAPK/ERK, upregulating MyoD and protein synthesis (Philippou et al., 2007).
LESS TECHNICAL EXPLANATION
PEG-MGF activates IGF-1 receptors, triggering pathways that support cell survival and muscle growth.
POTENTIAL RESEARCH EXPLORATIONS
Test synergy with IGF-1/HGF, explore cardiac repair, or optimize nerve dosing (Philippou et al., 2007).