T Nation

IGF Critic

a discussion from another forum was curious to see what people on here thoughtWith my experience with igf i must say i disagree.,…this is from RR on MD

After many years of making countless posts on LR3 IGF-1, I’ve finally tired of the topic.
This will be my last post ever on LR3 IGF-1.

  1. Gropep,who invented LR3 IGF-1, altered the protein chain for prolonged lab experiments. Once the protein chain was altered, IGF-1 lost it’s muscle building properties once converted to LR3 IGF-1

2)Yes, some legit research has shown that IGF can multiply muscle fiber, but there is ZERO research on LR3 IGF-1, nor will there ever be. It was meant for lab cultures only

  1. Should you get IGF-1, it is rendered useless by using acetic acid, since you need the correct pH and ionic environment for the peptide chains to unwind. HCL is what’s needed.

4)The bulk of the response to IGF comes from it’s ability to act as a sensational glucose disposal agent. This is the part where IGF’s name, “Insulinlike”, comes to the fore.

  1. I’m convinced any weight gain on LR3 IGF-1 is an uptick in glycogen/ water retention.

  2. Myself, along with several friends ,conducted studies on ourselves running LR3 IGF-1 at 3 different doses. Since LR3 IGF-1 is touted as some miracle mass builder, we never used steroids in our experiments. At 100 mcg, 150 mcg, and 200 mcg no one experienced muscle gains after 4 weeks on. Yes, we had hydrostatic testing done before during and after each experiment.

I think you get my point …no more LR3 IGF-1 debate for me. You want to piss your money away, go for it.

~RR

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I however had great success with my first run with IGF. Possibly placebo effect but I really got good strength and size gains in only three weeks.

My last run was barely even noticable. Perhaps the quality of the IGF sold by various companies could be called into question.

Well I can tell you that native human IGF-1 dissolved in a neutral pH solution like phosphate buffered saline (my personal favorite) at a high concentration (over 1 mg/mL) will do things when injected into specific tissues.

It is not a complete waste… the LR3 and acid solutions rendering it useless I have no idea about. Although IGF-1 has 3 disulfide bonds that should keep it relatively stable to misfolding in any sort of solution, so I have a hard time believing an acid solution would ruin it.

However acidic solutions suck to inject and I would not suggest using an acidic solution to dissolve & inject peptides to anyone.

[quote]sota123 wrote:
3) Should you get IGF-1, it is rendered useless by using acetic acid, since you need the correct pH and ionic environment for the peptide chains to unwind. HCL is what’s needed.
[/quote]

I am going to have to disagree with this. As I stated above I wouldn’t use an acid solution to dissolve & inject any peptide, so this is really irrelevant to me, but how can you say that you need the correct pH and ionic environment for the peptide (protein, actually) chains to unwind?

Are you assuming that IGF-1 aggregates into inactive multimers if you put it in the wrong solution? Native IGF-1 is unlike native insulin in that it does not hexamerize in solution or upon injection. This is the basis for Humalog.

Hydrochloric acid and acetic acid will not have any effect on the solution-state of IGF-1 molecules. There is no “peptide chain unwinding” that needs to take place. IGF-1 is highly stabilized by its preexisting disulfide bonds and these bonds, which are required for receptor affinity & activation, will ensure that the protein remains in a useful conformation as long as it is not degraded.

Only 1 person cares to rebut this? I wonder, is that because not many people try LR3, or because it doesn’t do much.

[quote]Rusty Barbell wrote:
sota123 wrote:
3) Should you get IGF-1, it is rendered useless by using acetic acid, since you need the correct pH and ionic environment for the peptide chains to unwind. HCL is what’s needed.

I am going to have to disagree with this. As I stated above I wouldn’t use an acid solution to dissolve & inject any peptide, so this is really irrelevant to me, but how can you say that you need the correct pH and ionic environment for the peptide (protein, actually) chains to unwind?

Are you assuming that IGF-1 aggregates into inactive multimers if you put it in the wrong solution? Native IGF-1 is unlike native insulin in that it does not hexamerize in solution or upon injection. This is the basis for Humalog.

Hydrochloric acid and acetic acid will not have any effect on the solution-state of IGF-1 molecules. There is no “peptide chain unwinding” that needs to take place.

IGF-1 is highly stabilized by its preexisting disulfide bonds and these bonds, which are required for receptor affinity & activation, will ensure that the protein remains in a useful conformation as long as it is not degraded.
[/quote]

I think the original poster was somehow assuming that a protein needs to be “unwound” or “open” or unfolded to exert its effects. He assumed that the folded state is the inactive state. Obviously, that’s retarded as protein unfolding is what kills enzyme activity. But you pretty much covered everything.