Comparison
MGF (Mechano Growth Factor) vs. Tesamorelin
Two peptides side-by-side — identity, evidence base, legal status and known adverse events.
Identity
Category
Growth
Growth
CAS no.
12-Aminosäuren-C-terminales E-Domänen-Peptid (Sequenz nicht standardisiert)
901758-09-6
Molecular weight
2867.2 g/mol
5135.83 g/mol
Half-life
0.1 h
0.4 h
Sequence
YQPPSTNKNTKSQRRKGSTFEERKtrans-3-hexenoyl-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly-Ala-Arg-Ala-Arg-Leu-NH2Mechanism of action
MGF (Mechano Growth Factor)
The IGF-1 gene produces multiple isoforms by alternative splicing. IGF-1Ec is upregulated after mechanical muscle loading; the C-terminal E-domain is cleaved from the mature IGF-1 protein and appears to have independent effects on satellite cells. The exact receptor binding of the E-domain is not established; a classical IGF-1R effect is unlikely since mature IGF-1 is responsible. In cell-culture studies, stimulation of myoblast proliferation and differentiation has been observed.
Tesamorelin
Tesamorelin is an N-terminally modified 44-amino-acid version of human GHRH(1-44). A 3-hexenoyl modification protects against rapid dipeptidyl-peptidase-IV cleavage. Binding to the pituitary GHRH receptor stimulates endogenous pulsatile growth-hormone secretion and consequently hepatic IGF-1 production.
Evidence base
Highest evidence
Animal model
Human RCT
Studies
4
2
of which in humans
0
2
Effects recorded
3
3
Open conflicts
0
0
Documented adverse events
1
2