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Peptide Sciences Blog

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Epithalon Fights Aging by Activating Telomerase and More

By Logan E. 2 years ago

Epithalon Fights Aging by Activating Telomerase and More

Epithalon (epitalon) is a four-amino-acid-long peptide derived from a naturally occurring pineal gland protein. It has been shown, through extensive animal research, to be a potent regulator of cell metabolism, including growth and cell division. In particular, epithalon is able to extend cell survival in vitro. At least part of the reason that epithalon can extend cell survival comes down to its action on telomeres.

Telomeres

Telomeres, the repetitive nucleotide sequences at the end of linear chromosomes, protect DNA from degradation and deterioration. A telomere sequence starts out at about 11,000 DNA units (bases) long, but decreases in length to about 4,000 bases in old age. Interestingly, the rate of telomere degradation is faster in men than in women.

Telomeres are like self-sacrificing guards against actual DNA damage. Because they don’t code for anything, telomeres can be sacrificed when DNA is replicated (copied) without actually damaging any genes. This is necessary because DNA replication is an imperfect process. Of course, telomeres eventually get too short to serve their protective role. Cells have mechanisms to detect when this happens. When a telomere becomes too short, the cell either becomes inactive or dies. This is essentially the process of aging at a molecular level.

Peptides: What are they?

By L. Johnston 3 years ago

Peptides: What Are They?

Peptides are biological materials that are made from building blocks called amino acids. Animals get most of their amino acids from the foods they eat. Different cells then assemble these amino acids into long chains called peptides or proteins. As the chains grown in length, they are able to fold back on themselves. As it turns out, certain amino acids can interact with one another when peptide chains fold. This results in the folds being locked into place, under normal physiologic conditions, which gives the peptide chain a three-dimensional structure. The length of the peptide chain as well as the order of the amino acids in it determines how the peptide folds and thus its ultimate three dimensional structure.

Receptors, special biological machines to which proteins can bind, will only accept proteins that have the right order of amino acids and the right three dimensional shape. By varying these two properties, it is possible to create proteins that have specific and very diverse functions. Research studies have shown that the peptide that binds to receptors in the heart, for instance, may not interact at all with receptors in the stomach or lungs. This allows for very specific signals to be sent from one region of the body to another, which allows for coordinated actions such as immune function, carbohydrate metabolism, and so forth.

Small Peptides

There is no formal definition for what makes a peptide “small,” but they often don’t have much in the way of three-dimensional structure. They may have a fold or two, but that is about it. These peptides rely more on their amino acid sequence than their 3-D structure for signaling. Even a small change in the order of the amino acids of a small peptide (or even the number) can make a huge difference in terms of the receptors that it can bind to. Sometimes, a change of just a single amino acid is enough to completely alter the function of a small peptide.

In the past, most of the research focus was on larger peptides and massive proteins. This was because most scientists thought that biologically active proteins were large. It was also thought that the best way to develop therapeutics was to exactly mimic existing proteins. This approach, however, isn’t entirely accurate.

New research is indicating that small peptides are not only easier to make; they can also have a wide range of biological activity. It is no longer thought that mimicking naturally occurring proteins is the best way to develop therapeutics. Science has now shifted its focus to small peptides and their potential. This shift makes sense given that small peptides have been shown to have applications ranging from antibiotics and heart medications to preventative solutions for diseases like diabetes. They have even been shown to have anti-aging effects in animal models.

The Future of Small Peptides

It is clear that the future of medicine will be rife with small peptides. They won’t be the only therapeutics available, but they will continue to make up a larger and larger percentage of the substances we use to promote health. Most importantly, small peptides can be custom-made to fight off disease and preserve health. They are less complicated to synthesize and produce and what we learn from early research trials will certainly inform us moving forward. Within a decade or two, small peptides will be as common in the medical field as antibiotics and vaccines are today.