LakeMountD
Doctor Science
- Awards
- 1
I know a lot of you out there are really confused on everything that is going on with these peptides and I can assure you it tends to hit me pretty hard too when I begin researching them, unfortunately, IBE and I are absolutely obsessed with peptides to the point we will probably both join the same peptide rehab group soon haha.
I wanted to talk a little bit about why I feel the current version of MGF isn't really working and the use of a PEG molecule to fix the problem.
MGF, as it is being currently sold, is getting a bad rep from people due to the fact they feel that they are not seeing gains from it. Many people believe that the use of MGF in their cycles or protocols just flat out won't work, however, this is far from the truth. It isn't that MGF isn't working but, instead, because the molecule isn't able to survive long enough to exhibit its effects in the body. As some of you PubMed junkies know there aren't a lot of studies on Mechano Growth Factor (I say this because there are other types of MGF's) and there is only one of which that I have found that talks about its half life. The half life of MGF is said to be shorter than that of hIGF-1, which in multiple studies has been said to be ~20 minutes. Your body's biochemical solution to this is the introduction of IGFBP's or IGF Binding Proteins, which bind to IGF-1 and render it inactive, all the while preserving its half life as well; when the body is in need of more IGF-1, the levels of IGFBP's falls and plasma levels of IGF-1 once again increases. MGF, on the other hand, does not bind the IGFBP's despite MGF being a spliced variant of IGF-1. In one study conducted by Goldspink, he refers to a type of protein that does keep the half life of MGF extended. He more or less uses deductive reasoning to say that this is the only other thing that is left that could bind to MGF and MGF has to have something to keep it from being degraded after < 20 min., therefore, we propose it is this. Since our bodies do not product an amount of MGF similar to that at which we inject, it is hard to say what happens to the MGF once we inject dosages such as 100mcg x 2 bilaterally. If the half life is roughly 10 minutes, it would be absolutely impossible for the mechanism by which MGF acts through to cause rapid proliferation, since the MGF would quickly saturate the area it was injected and deplete its resource pathway, and it also seems improbable for the body to have enough proteins to keep the MGF from degrading, since it is not used to the large influx of exogenous MGF.
Now that we have talked about the problem of MGF's half life (we will touch on how to fix this problem later), lets begin to talk about another aspect of MGF's eventual demise: packaging/shipping/storage. One of the biggest misconceptions people seem to have is that LR3 IGF-1 and MGF are very similar and, therefore, would act similar in solution and in the body. This is about as far from the truth as it gets. If you think to substances such as L-Carnitine compared to Acetyl-L-Carnitine you can see the vast difference a small addition can make to a molecule. An acetyl group is merely a CH3 group attached to a carbon that is double bonded to an oxygen, not much of a difference, especially when very large proteins (with 50+ carbons already attached) but the effects can be largely different. LR3 IGF-1 was designed by GroPep International, a company who marketed the product for scientific and possible pharmaceutical use. They created a protein sequence that prevented rapid enzymatic degredation (destruction of the molecule by the body), which increased the half life. MGF does not have any such addition. MGF does act a lot like IGF-1Ea, however, IGF-1Ea is vastly different than LR3 IGF-1 in the way it acts in the bloodstream. MGF is actually water soluble, unlike LR3 IGF-1, and again unlike LR3 IGF-1 it is very unstable in solution. According to Sigma and Phoenix Peptides, MGF MUST be kept below freezing to prevent peptide degradation, once you go above a certain point you will severely limit the mass of active peptide that you receive. Once reconstituted MGF must be kept as close to freezing as possible, since water freezes at 0*C and it is water soluble it must be kept above 0*C. At this temperature it is suggested that the peptide will last ~1 week. Phoenix has stated that, although no studies have been done on MGF once reconstituted, they recommend refreezing it at -70*C. I don't know about you but I don't have access to liquid nitrogen so that I can refrigerate something to those levels! Not only that but this process can only be done once as repetitive freezing/thawing can cause further peptide degredation. Reconstituted MGF will last ~3-6 months when refrigerated at -70*C. Phoenix has also stated that shaking of the bottle or even constant vibrations (which can be caused by loud bass as well) will also degrade the peptide, but it is mostly stable (for only on week) if kept near freezing based on structure.
So lets assume for moment that someone who has synthesized your MGF, walked it to you as slowly as possible without shaking it or disturbing it in any way, kept it below freezing the entire time, reconstituted it and kept it at 0.1*C in a pitch black refrigerator, you would still only have 1 week to use it all up! Do you really feel that a peptide, which is NOT a hormone, can really give you results this quickly? Definitely not. It is almost impossible that the peptide is shipped by the company who created it to the person who ordered it and it is kept completely dry and below freezing (often coming from China), and therefore once again some peptide degredation as occurred. Then when shipping to you, again it is near impossible to keep the temperature cold enough to prevent degredation and your mass% of MGF is continuing to fall.
Now after all this pessimistic talk what can be done? MGF has a couple different forms, one of which is a d-arg substituted version. Some forms of MGF are more stable than others and still have their functional group intact and work in the same manner. Instead of altering the MGF protein sequence, however, it is better to use something called pegylation. Pegylation uses a substance called polyethylene glycol, which can be attached to a protein molecule and create a "shield" around the protein itself to prevent things such as enzymatic degredation and rapid glomerular excretion while decreasing immunogenicity (the rate at which the substance causes an immune response) and increasing overall half life. This is achieved through the unique structure of ethylene glycol. It creates a steric hindrance (which is basically a large negatively charged shield that pushes away other negatively charged particles, much in the same way two negatively charged magnets repel each other when you push them together) around the protein or peptide and protects clevage points (which are poitns at which the enzyme can attack the peptide and break it in half so to speak) while NOT blocking the are where the peptide/protein attaches to the receptor. Think of it as a raincoat that protects you from the rain but still has small holes for your hands, feet, and face. Depending on the size of the molecule, depends on what size PEG molecule you want to use. PEG weights vary greatly. Too large of a PEG and you can actually block the receptor binding site. However, if the right weight is chosen, it can have profound effects on protein/peptide stability and a reduction in toxicity. Even if the peptide/protein itself is not water soluble, many times the addition of PEG will create a water soluble compound.
The half life of a PEG molecule can be enhanced greatly. Instead of the < 20 minute half life of regular MGF, pegylated MGF can have a half life of many days, although the exact half life is not know. This has brought scientists such as Yang and Goldspink, who lead their field in IGF-1 Axis research, to use pegylated MGF in their studies as opposed to regular MGF to increase experimental accuracy with the extended stability and half life. This would allow someone to inject PEG MGF twice or possibly once per week while not having to worry about peptide degredation in solution as PEG molecules repel away from themselves as well. The only difference now, is that instead of a localized MGF, we have the possibility of a systemic MGF, which COULD be detrimental, but it is yet to be seen as we have not yet tested this theory. At the correct dosage it could work out VERY VERY well as it would allow total body proliferation, but if taken in too high dosages, could inhibit differentiation.
Bottom line, dump the current MGF versions, biopharmaceuticals are the way of the future and PEG structures have shown VERY significant results in current pharmaceutical drugs. I see PEG MGF being a great supplement and we should look more to these longer lasting peptides/proteins such as LR3 IGF-1, MGF, and many others to come!
I wanted to talk a little bit about why I feel the current version of MGF isn't really working and the use of a PEG molecule to fix the problem.
MGF, as it is being currently sold, is getting a bad rep from people due to the fact they feel that they are not seeing gains from it. Many people believe that the use of MGF in their cycles or protocols just flat out won't work, however, this is far from the truth. It isn't that MGF isn't working but, instead, because the molecule isn't able to survive long enough to exhibit its effects in the body. As some of you PubMed junkies know there aren't a lot of studies on Mechano Growth Factor (I say this because there are other types of MGF's) and there is only one of which that I have found that talks about its half life. The half life of MGF is said to be shorter than that of hIGF-1, which in multiple studies has been said to be ~20 minutes. Your body's biochemical solution to this is the introduction of IGFBP's or IGF Binding Proteins, which bind to IGF-1 and render it inactive, all the while preserving its half life as well; when the body is in need of more IGF-1, the levels of IGFBP's falls and plasma levels of IGF-1 once again increases. MGF, on the other hand, does not bind the IGFBP's despite MGF being a spliced variant of IGF-1. In one study conducted by Goldspink, he refers to a type of protein that does keep the half life of MGF extended. He more or less uses deductive reasoning to say that this is the only other thing that is left that could bind to MGF and MGF has to have something to keep it from being degraded after < 20 min., therefore, we propose it is this. Since our bodies do not product an amount of MGF similar to that at which we inject, it is hard to say what happens to the MGF once we inject dosages such as 100mcg x 2 bilaterally. If the half life is roughly 10 minutes, it would be absolutely impossible for the mechanism by which MGF acts through to cause rapid proliferation, since the MGF would quickly saturate the area it was injected and deplete its resource pathway, and it also seems improbable for the body to have enough proteins to keep the MGF from degrading, since it is not used to the large influx of exogenous MGF.
Now that we have talked about the problem of MGF's half life (we will touch on how to fix this problem later), lets begin to talk about another aspect of MGF's eventual demise: packaging/shipping/storage. One of the biggest misconceptions people seem to have is that LR3 IGF-1 and MGF are very similar and, therefore, would act similar in solution and in the body. This is about as far from the truth as it gets. If you think to substances such as L-Carnitine compared to Acetyl-L-Carnitine you can see the vast difference a small addition can make to a molecule. An acetyl group is merely a CH3 group attached to a carbon that is double bonded to an oxygen, not much of a difference, especially when very large proteins (with 50+ carbons already attached) but the effects can be largely different. LR3 IGF-1 was designed by GroPep International, a company who marketed the product for scientific and possible pharmaceutical use. They created a protein sequence that prevented rapid enzymatic degredation (destruction of the molecule by the body), which increased the half life. MGF does not have any such addition. MGF does act a lot like IGF-1Ea, however, IGF-1Ea is vastly different than LR3 IGF-1 in the way it acts in the bloodstream. MGF is actually water soluble, unlike LR3 IGF-1, and again unlike LR3 IGF-1 it is very unstable in solution. According to Sigma and Phoenix Peptides, MGF MUST be kept below freezing to prevent peptide degradation, once you go above a certain point you will severely limit the mass of active peptide that you receive. Once reconstituted MGF must be kept as close to freezing as possible, since water freezes at 0*C and it is water soluble it must be kept above 0*C. At this temperature it is suggested that the peptide will last ~1 week. Phoenix has stated that, although no studies have been done on MGF once reconstituted, they recommend refreezing it at -70*C. I don't know about you but I don't have access to liquid nitrogen so that I can refrigerate something to those levels! Not only that but this process can only be done once as repetitive freezing/thawing can cause further peptide degredation. Reconstituted MGF will last ~3-6 months when refrigerated at -70*C. Phoenix has also stated that shaking of the bottle or even constant vibrations (which can be caused by loud bass as well) will also degrade the peptide, but it is mostly stable (for only on week) if kept near freezing based on structure.
So lets assume for moment that someone who has synthesized your MGF, walked it to you as slowly as possible without shaking it or disturbing it in any way, kept it below freezing the entire time, reconstituted it and kept it at 0.1*C in a pitch black refrigerator, you would still only have 1 week to use it all up! Do you really feel that a peptide, which is NOT a hormone, can really give you results this quickly? Definitely not. It is almost impossible that the peptide is shipped by the company who created it to the person who ordered it and it is kept completely dry and below freezing (often coming from China), and therefore once again some peptide degredation as occurred. Then when shipping to you, again it is near impossible to keep the temperature cold enough to prevent degredation and your mass% of MGF is continuing to fall.
Now after all this pessimistic talk what can be done? MGF has a couple different forms, one of which is a d-arg substituted version. Some forms of MGF are more stable than others and still have their functional group intact and work in the same manner. Instead of altering the MGF protein sequence, however, it is better to use something called pegylation. Pegylation uses a substance called polyethylene glycol, which can be attached to a protein molecule and create a "shield" around the protein itself to prevent things such as enzymatic degredation and rapid glomerular excretion while decreasing immunogenicity (the rate at which the substance causes an immune response) and increasing overall half life. This is achieved through the unique structure of ethylene glycol. It creates a steric hindrance (which is basically a large negatively charged shield that pushes away other negatively charged particles, much in the same way two negatively charged magnets repel each other when you push them together) around the protein or peptide and protects clevage points (which are poitns at which the enzyme can attack the peptide and break it in half so to speak) while NOT blocking the are where the peptide/protein attaches to the receptor. Think of it as a raincoat that protects you from the rain but still has small holes for your hands, feet, and face. Depending on the size of the molecule, depends on what size PEG molecule you want to use. PEG weights vary greatly. Too large of a PEG and you can actually block the receptor binding site. However, if the right weight is chosen, it can have profound effects on protein/peptide stability and a reduction in toxicity. Even if the peptide/protein itself is not water soluble, many times the addition of PEG will create a water soluble compound.
The half life of a PEG molecule can be enhanced greatly. Instead of the < 20 minute half life of regular MGF, pegylated MGF can have a half life of many days, although the exact half life is not know. This has brought scientists such as Yang and Goldspink, who lead their field in IGF-1 Axis research, to use pegylated MGF in their studies as opposed to regular MGF to increase experimental accuracy with the extended stability and half life. This would allow someone to inject PEG MGF twice or possibly once per week while not having to worry about peptide degredation in solution as PEG molecules repel away from themselves as well. The only difference now, is that instead of a localized MGF, we have the possibility of a systemic MGF, which COULD be detrimental, but it is yet to be seen as we have not yet tested this theory. At the correct dosage it could work out VERY VERY well as it would allow total body proliferation, but if taken in too high dosages, could inhibit differentiation.
Bottom line, dump the current MGF versions, biopharmaceuticals are the way of the future and PEG structures have shown VERY significant results in current pharmaceutical drugs. I see PEG MGF being a great supplement and we should look more to these longer lasting peptides/proteins such as LR3 IGF-1, MGF, and many others to come!
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