.gif "IP Gear")
- Joined
- Feb 16, 2006
- Messages
- 1,051
We are the first and only company with human PEGylated MGF and all our peptides are synthesized in the USA
PEGylated Mechano Growth Factor is a new and innovative form of MGF that outperforms natural MGF many times over. PEGylation technology was introduced into the pharmaceutical industry more recently to virtually eliminate the problems associated with biopharmaceuticals. Biopharmaceuticals have a lot of negative issues associated with them that make their use limited in the pharmaceutical industry, such as extremely short half-lives caused by proteolytic degradation (often not exceeding 2 minutes), increased renal (kidney) excretion, and inactivation of the peptide caused by your body’s natural immune response. This problem, however, is corrected by attaching different PEG molecules to proteins and peptides. PEG stands for polyethylene glycol, a unique polymer that is non-ionic and soluble in water. By covalently bonding a PEG chain to a peptide you can expand the physical radius of the overall molecule, which creates a “shield” around the peptide and prevents proteases and antibodies from cleaving it and rendering it inactive. PEGylation also has various lengths (weights) and using a chain that is too large can block the binding of the peptide to its receptor. This, and the fact that MGF is a smaller peptide, is why we decided to use a smaller PEG chain and since d-arg MGF is insoluble in water the addition of a PEG chain is a positive feature to this peptide. This prevents the need for acidic solutions and provides a virtually painless injection.
Our PEG MGF is also unique in the sense that we did not go with a PEG molecule attached to a normal human MGF peptide. Instead, we decided to use 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, we eliminate this problem and extend the half life well beyond basic hMGF. Our PEG MGF also contains another unique addition to its structure. By looking at the difference between hMGF and our 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.
What does all of this science-talk do for you? Greater stability of the MGF peptide, less susceptibility of cleavage from various enzymes, decreased immune response, and decreased excretion rate in the kidneys, all of which greatly increase the half-life of the peptide. hMGF has a half life of less than 20 minutes in the body, but with various technologies that we have added we can extend this half life from minutes to days!
