I’m not sure that 0.9% benzyl alcohol will destroy these peptides, but yes, they are more sensitive to this kind of exposure—at least according to ChatGPT. No precise experiments have been conducted to empirically prove this.
The reason IGF-1 (LR3 and DES) need Acetic Acid (AA) is because every peptide has an Isoelectric Point. This is the point where the molecule has a neutral or zero electrical charge. The pI of IGF-1 is naturally basic at around 8.4~. When it is in a solution with a pH close to its pI, the molecules lose their electrical repulsion and start clumping together (aggregation) and can physically stick to the spores of the glass vial (adsorption). Sounds a bit wild, but you will lose the peptide to the glass.
When in 0.6% AA, the pH drops to roughly 2.5 to 3.0. In this highly acidic environment, you are putting the molecules far away from it's pI, so they become heavily positively charged. Because positive repels positive, the molecules repel each other and essentially bounce off the glass.
** And going back to Follistatin - I was wrong. The molecule is a very large complex glycoprotein and must maintain that specific 3D folded shape to physically grab and neutralize Myostatin in your body. This molecule is held together very a delicate electrostatic bond (salt bridges) and hydrogen bonds.
Where I was wrong was when you introduce this protein into a highly acidic environment (pH less than 3.0), the influx of hydrogen ions (H+) disrupt and break the salt bridges causing it to basically... unfold. This is called denaturation. So do
NOT add Follistatin to something that will make it lose its 3D shape. So, yes I have went back and updated my library of notes. I was wrong on that one.
Beautiful picture huh (don't laugh). AA hurts, but you can get used too it over time. There is a method called backloading where you draw your IGF analog out of the reconstituted AA, getting your precise dose, then drawing up some BAC right before injecting if you are really trying to avoid to punch of AA.