Peg Mgf (2mg)

PEG MGF is also unique in the sense that it is not a PEG molecule attached to a normal human MGF peptide. Instead, there is a more stable form of the peptide, a variant with 2 d-arg substitutions at positions 14 and 15, where there was once the natural l-arg. These additions create a more stable peptide in itself, since basic l--arg-l-arg bonds are easily cleaved by proteases in the blood. By creating a d-arg-d-arg bond, instead, problem is eliminated and extends the half life well beyond basic hMGF. PEG MGF also contains another unique addition to its structure. By looking at the difference between hMGF and PEG MGF, one of the first things you will notice is the addition of an NH2 group at the C-terminal (right) side of the peptide. This amine addition is often used by pharmaceutical companies to, once again, increase the half life of the peptide by making it less susceptible to carboxypeptidases in plasma, which are enzymes that remove amine (NH2) groups from the end of peptides and render them inactive. Since all peptides have a Carboxyl (COOH) and amine (NH2) group attached to the ends of them, the addition of another amine group to the end of the carboxyl side of the peptide greatly decreases the chances of the functional amine group getting cleaved by enzymes. In most cases this addition has no effect on the peptide’s interaction with its receptor.