Livagen is a short peptide bioregulator, similar in structure to Epitalon. It is a tetrapeptide made of the amino acids Lys-Glu-Asp-Ala (KEDA) and is classified amongst Khavinson’s peptides. As a bioregulator, the peptide may interact with genetic material in different cells and consequently unpack and “unlock” various cellular genes. Livagen’s impacts appear to be exhibited directly on the lymphocytes (cells of the immune system), liver, and gastrointestinal tract (GIT). Its direct functions may be widespread, as suggested through research studies on DNA and gene expression patterns. The potential of the Livagen peptide to activate genes enclosed in the GIT and immune system may reflect possible age-mitigating characteristics exerted on cells.

Cardiogen is a cardiovascular bioregulator peptide complex. Results obtained from research studies suggest that Cardiogen’s primary functions may be correlated to fibroblast action, cells considered responsible for scar formation and tissue repair. The peptide has a sequence of H-Ala-Glu-Asp-Arg-OH (AEDR).^[1] Research posits that the synthetic tetrapeptide Cardiogen may potentially stimulate cell proliferation in myocardial tissue. Additionally, it appears that Cardiogen may possibly inhibit myocardial cell apoptosis (cell death), hypothetically through the reduction of p53 protein expression.

Syn-AKE is a peptide, also known as tripeptide-3 or dipeptide diaminobutyroyl benzyl amide diacetate. Syn-AKE, a synthetic peptide ingredient, appears to mimic the actions of the Waglerin-1 peptide, which is 21 amino acids in length. Waglerin-1 functions primarily as a muscle relaxant by inhibiting the activity of acetylcholine at the neuromuscular junction, which may potentially result in reduced muscle contractions. Acetylcholine is a neurotransmitter considered essential for muscle movement, and its inhibition at the neuromuscular junction prevents the normal contraction signals from reaching muscles. In the development of Syn-AKE, researchers sought to synthesize a peptide that might potentially mimic this action. Thus, the peptide Syn-AKE was engineered to emulate the mechanism by which Waglerin-1 acts, but in a more selective manner. Researchers suggest Syn-AKE may act to reduce transmission between muscles and nerves, working similarly to botulinum toxin to relax muscles and thus reduce instances of creasing and wrinkle development along epidermal surfaces, as suggested in animal model research. The apparent reduction of this transmission appears to be reversible when triggered by Syn-AKE. Therefore its action is temporary.^[1] According to Pentapharm, “the Syn-AKE invokes its action by blocking the muscle nAChR in a reversible manner by blocking the ion channel. As a result, the Na+ uptake is substantially disturbed, and the muscles remain relaxed.”

AICAR or 5-Aminoimidazole-4-carboxamide ribonucleotide, is a synthetic adenosine monophosphate analog. It was developed to stimulate the AMP-dependent protein kinase (AMPK) activity.^[1][2] It is currently being investigated as a protective agent against ischemic damage in the cardiac myocytes during cardiac injury. The AMP-activated protein kinase is an enzyme and a protein that may play a regulatory role in several metabolic pathways. Its expression has been observed in several tissues, including the skeletal muscles, liver, and brain. In all these tissues, it is considered to exert a potential net effect on lipogenesis and may inhibit cholesterol synthesis and ketogenesis. It may also modulate insulin secretion and skeletal muscle fatty acid oxidation with glucose uptake. Several energy deficit states may trigger the release of AMPK, like hypoxia or hypoglycemia.

GHK-Cu (Copper Tripeptide) is a tripeptide that scientists assert is naturally present in blood plasma. It has a sequence of Gly-His-Lys (glycine, histidine, and lysine,) which readily binds with copper to form the copper tripeptide. Scientific studies carried out in different research laboratories worldwide have explored its various biological roles. GHK-Cu exhibits some potential to influence various biological pathways, including an apparent induction of tissue repair, attraction of immune cells, antioxidant and anti-inflammatory characteristics, activation of collagen and glycosaminoglycan synthesis in skin fibroblasts, regulation of extracellular matrix components like decorin, and possible promotion of blood vessel growth. Recent studies indicate its potential role in stem cell biology and anti-tumor research as well.

Follistatin-344 is a synthetic, full-sized version of a naturally occurring protein bearing the same name. Follistatin-344 occurs in two isomers, varying based on their gene splicing. Follistatin may exist endogenously in two distinct variants, referred to as FST 317 and FST 344. The variants are distinguished by their composition: FST 317 comprises 288 amino acids, whereas FST 344 comprises 315 amino acids. The numerical part of their names reflects the number of amino acids in the precursor molecules from which they are synthesized, with the precursor to FST 317 having 317 amino acids and that to FST 344 having 344 amino acids. It appears that FST 344 is the more commonly occurring form across various tissues. On the other hand, the FST 317 variant likely represents a minor fraction, potentially comprising under 5% of the total mRNA transcript related to Follistatin. Thus, Follistatin-344 appears to be the main constituent. Researchers suggest that its primary role may be to counteract the action of the Tumor Growth Factor-beta (TGF-beta) family. The TGF-beta family comprises Myostatin, Activin, and Follicle Stimulating Growth Hormone (FSH). Follistatin-344 appears to stimulate the Insulin/IGF-1 pathway, and the reported immense potential of the peptide has been published in Follistatin-344 research.

Tripeptide-29 is a peptide that is one of the basic monomers of collagen. Collagen is a long-chain polymer composed of short monomers made of three consecutive amino acids. These monomers combine to form a secondary structure, which then may form tertiary and even quaternary structures. These complex structures may have many potential emergent properties. For example, most collagen molecules are thought to play roles in providing structural integrity and elasticity to the cellular complexes in tissues like the stratum corneum, tendons, and bones.

Collagen subunits most often follow the pattern of Gly-Pro-X, Gly-Xo-X, or Gly-X-Hyp. Tripeptide-29 is a GlyPro Hyp peptide, a complete synthetic analog of common collagen building blocks. Beyond its proposed involvement in collagen synthesis, researchers speculate that Tripeptide-29 may have additional biological implications. For instance, some preliminary studies suggest it may act as an antioxidant, potentially aiding in the protection of cells against oxidative stress, which is the imbalance between free radicals and antioxidants that may lead to cellular damage.

It is hypothesized that Tripeptide-29 might exhibit anti-inflammatory properties, possibly reducing inflammation; anti-fibrotic actions, which may help mitigate excessive formation of fibrous connective tissue; and anti-melanogenic characteristics, potentially influencing melanin production and affecting pigmentation processes in the dermal and epidermal layer.

SNAP-8, or Synaptosomal-associated protein 8, is a synthetic octapeptide believed to mimic certain functionalities of its larger counterpart, SNAP-25, a protein deemed integral to neurotransmitter release and muscle contraction.^[1] Constructed from eight amino acids, SNAP-8’s structure is designed with specific modifications: an acetylated N-terminus and an amidated C-terminus, culminating in the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2. It is structurally similar to another peptide known as acetyl hexapeptide-3, which also reportedly mimics a fragment of SNAP-25 and inhibits its function, leading to similar anti-wrinkle potential. By adding two amino acids to the chain of acetyl hexapeptide-3, the resultant acetyl octapeptide further enriches the field of research compounds studying cell aging and skin cell rejuvenation.^[2]

The synthesis and manufacturing of SNAP-8 comprises a final freeze-drying step called lyophilization. Generally, the crystalline powder obtained due to freeze-drying is in the form of a polymorphous compound. It may be present in aggregates and show variation in the crystal size. However, this does not appear to lead to any chemical discrepancy in its composition. Extensive experimental studies have supported the homogeneity of this compound. The usual shelf life of SNAP-8 is posited to be at least 12 months, provided the compound is stored in a clean, cool, and dry place. If the compound is intended to be stored longer than a year, the temperature should be maintained at 4 degrees Celsius. This may extend the shelf life to approximately 18 months. Refrigeration of the SNAP-8 may potentially lead to its precipitation; however, this doesn’t appear to change the integrity of the compound.