Sermorelin Part 1

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Sermorelin, also occasionally known as Geref, is a 29-amino acid polypeptide that is considered to be the shortest fully functional fragment of GHRH.  It has a molecular mass of 3357.882, and it has a molecular formula of C149H246N44O42S.

Sermorelin at a Glance

According to scientific study that has been conducted on animal test subjects, it has been determined that the primary functionality of Sermorelin correlates with the relationship that it possesses with the pituitary gland.  This is the pea-sized gland located at the bottom of the hypothalamus at the base of the brain that is responsible for the regulation and control of a wide array of endocrine system-related processes, including growth, metabolism, temperature regulation, sex organ functionality, and more.

Scientific study based on animal test subjects has determined that Sermorelin’s presence produces a stimulation of secretions related to muscular and skeletal tissue growth directly from the pituitary gland.  This boost in secretions allows an animal test subject to achieve homeostasis regarding its muscular and skeletal tissue on a more efficient basis.

It should be noted that because Sermorelin works directly with the pituitary gland when it comes to stimulating specific secretions, its functionality is a little different than other peptides that are classified as GHRH.  For instance, some peptides that land within the GHRH realm promote an increase in muscular and skeletal tissue growth by increasing the expression of IGF-1, or Insulin Growth Factor – 1, which is secreted by the liver.  However, Sermorelin produces a means of muscular and skeletal tissue growth promotion directly through pituitary gland stimulation via the binding of specific receptors.  The subsequent expressions that occur stem directly from the pituitary gland and not through a secondary agent.  This direct link causes the process to be regulated by negative feedback that correlates to the inhibitory neurohormone somatostatin.  Ultimately, this causation provides the animal test subject with a regulatory process that is more efficient and streamlined in nature.

Sermorelin and Functional Boosts

Because of the way in which Sermorelin operates in regards to the process of boosting the pituitary gland secretions that correlate to muscular and skeletal tissue growth, scientific study that has been conducted on animal test subjects has determined that the presence of the peptide could be responsible of a wide range of increased regulatory functions.

Some of these boosted functions include:

  • Muscle and skeletal tissue growth – because Sermorelin has been shown to be directly linked to an increase in secretions from the pituitary gland relating to muscular and skeletal tissue, it is thought that the process of muscular and skeletal tissue growth can occur on a far more efficient means.
  • Increased bone density – Because the presence of the peptide allows for a more efficient means of skeletal tissue growth, it is thought that the uptick in efficiency allows for bones to become stronger and sturdier. This could in turn make it easier for bones to withstand certain injuries such as breaks and fractures.
  • The reduction of body fat – Because of the way in which Sermorelin operates, it is thought that the peptide causes an increase in the overall efficiency of protein synthesis. This boost in the process could be potentially linked to a more efficient means of breaking down adipose tissue – that is, body fat – in order to keep up with the elevated process.  This not only could hypothetically lead to a burning off of excess body fat in animal test subjects, but it can also allow new adipose tissue to be burnt off quicker.
  • And improvement in deep sleep – It has been determined through scientific study based on animal test subjects that the processes that relate to the functionality of the pituitary gland occur during deep sleep. Because of this, it is thought that the presence of Sermorelin causes a more efficient means of achieving deep sleep, so that the animal test subject’s body may be able to have sufficient time to properly handle the boost in protein synthesis.

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Lipopeptide Part 2

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Physical and Storage Properties of Lipopeptide

Lipopeptide is typically presented as a sterile, pale yellow or light brown lyophilized cake. The peptide’s only inactive ingredient is sodium hydroxinde, and it is there in minimal quantities for the purposes of pH adjustment. The solution itself will range in color from light brown to pale yellow when it is ready for the animal test subject.

Lipopeptide should be shipped at room temperature, but should be stored at 4 degrees Celsius upon arrival to a strictly controlled environment such as a laboratory or a medical research facility. The solution should in turn be aliquoted and stored either at or below -20 degrees Celsius.

Lipopeptide and Pepducin

Scientific study based on animal test subjects has also focused their study on lipopeptides and their role as pepducins. In essence, pepducins are novel cell-penetrating peptides that function as intracellular modulators of signal transference from receptors to G proteins.

These particular forms of lipopeptides function due to their relationship with various lapidated fragments of G protein-coupled cellular loops that are used to modulate G-protein-coupled receptors, which are alternatively known as the following:

  • Seven-transmembrane domain receptors
  • 7TM receptors
  • Heptahelical receptors
  • Serpentine receptor
  • G protein-linked receptors (GPLR)

These receptors are representative of a large protein family of receptors which work by sensing molecules outside the cell and activating inside signal transduction pathways, which in turn leads to cellular responses.

It has been shown that a Pepducin molecule consists of a short peptide that is culled from a GPCR intracellular loop, which is llinked to a hydrophobic moiety; that is, a functional group of atoms or bonds within a molecular structure that is repelled by water. The structure that is formed allows these specific lipopeptides to tether within the cell membrane lipid bilyaer. Once this occurs, it can target the CPCR/G protein interface through a singular, intracellular alloseteric mechanism. In other words, it can hone in and engage the protein through a process where the protein is regulated through the binding of an effector molecule at a place apart from the protein’s active site.

Lipopeptide Dynamics

Based on scientific study on animal test subjects, it appears that the antimicrobial activity of lipopeptide is linked to the AUC/MIC ration (that is, area under the concentration-time curve/minimum inhibitory concentration) ratio for specific pathogens.

It has also been determined that Lipopeptide is reversibly bound to specific plasma proteins in a concentration-independent fashion.  Chief amongst these is serum albumin, which is the substance that is key to regulating the blood’s osmotic pressure.  Studies on animal test subjects have also determined that mean serum protein binding in subjects with cretinine clearance, or CLCR, at a rate greater than or equal to 30 mL/min was also comparable to what was observed in healthy subjects with regulated renal function.

Lipopeptide, Muscles, and Nerves

Other scientific study that has been based on animal test subjects have determined that the presence of Lipopeptide does have certain skeletal muscle effects, although it should be noted that there was no effects in related to either smooth muscle or cardiac muscle.  The skeletal muscle effects that were observed were marked by microscopic degenerative and regenerative changes and variable elevations in creatine phosphokinase, also known as CPK. That said, no fibrosis or rhabdomyolysis were observed in repeat-dose observations in rats and in dogs. Furthermore, all muscle effects that were recorded were completely reversed within 30 days of test cessation.

It was also determined that effects on peripheral nerves accompanied by significant losses of pattelar reflex, gag reflex, and the perception of pain were observed in animal test subject-induced Lipopeptide doses higher than those that were linked to skeletal myopathy. It was also demonstrated that while some of these conditions were clinically improved within two weeks after dosing cessation at a lower dosage, it was determined that higher dosages resulted in a minimal residual histological changes when measured in a 6 month time interval.

And tissue distribution studies in rats demonstrated that Lipopeptide is held within the kidney. However, it was also shown that the peptide appears to penetrate the blood-brain barrier on a minimal basis following both single and multiple doses.

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