Premium Peptides

Just like all supplements are not created equal, not all peptides are created equal either. The raw materials from which peptides are produced, the procedures by which they are manufactured, and the processes by which they are purified all affect quality. Much of the dedication to quality comes down to the ethos of the manufacturer. Afterall, some supplements have a good reputation because the people making them insist on using the best ingredients, the best equipment, and the best manufacturing practices. The same is true of peptides, so here is a look at some of the factors that should be considered when purchasing peptides to distinguish premium peptides from run-of-the-mill peptides and inferior peptides. The purer a peptide preparation is, the more certain the outcome of peptide research will be because pure peptides eliminate the possibility of confounding elements like contaminants or binders. Choosing a premium peptide could be the difference between successful research outcomes and complete disaster.

What Is a Premium Peptide?

Defining a premium peptide might seem like a difficult task, but it ultimately comes down to purity. A premium peptide is simply a peptide preparation that contains only the advertised peptide and nothing else. While this definition sounds simple enough, achieving high degrees of purity in the real world is anything but. Achieving 100% purity is an impossibility, but purities well above 99% can be attained with dedication.

For simple benchtop work in a chemistry lab, a moderate protein purity of 80% to 90% is often acceptable. For functional studies, such as X-ray crystallography, high purity levels of 95% to 99% become necessary. For therapeutic proteins used in treatments, animal studies, or clinical trials, the highest standard is always above 99%. The difference in time and resources invested to go from moderate to high to highest is not linear. At each step, the investment often increases by an order of magnitude or more.

Proteins that are not pure enough can lead to several problems including alterations in the 3-D structure of the protein that render it useless or, in very severe cases, dangerous. Obtaining premium peptides is thus critical to ensuring good science with repeatable results and is necessary for safety as well. To get to this point generally means using a multistep purification protocol that adds cost and complexity. Not only are some labs unwilling to undertake this degree of rigor, but some are also simply incapable due to lack of equipment or proper scientific expertise. Choosing a lab that is ISO 9001 certified is one step toward ensuring that it has the people and the equipment to produce a premium peptide product.

The best labs ensure that the best raw ingredients are utilized, but this is just an initial step in producing a premium product. Raw ingredients can be contaminated by residual solvents, byproducts, or side products from production. Sometimes these contaminants can be toxic and though it is impossible to make something 100% pure, impurities can be minimized through proper purification. How this purification is carried out depends on the nature of the peptide being produced, but it is possible to achieve 99% or greater purity with enough time and skill. Getting to this level requires not only taking the necessary steps to achieve purity but ensuring that each of those steps is carried out with the highest degree of fidelity. This means careful buffer preparation, proper adherence to cleanliness, and verification that the final product is as pure as it should be. Developing premium peptides is about diligence and adherence to the highest manufacturing standards from the very beginning to the process right up to the moment the peptide is bottled and shipped to the customer.

A peptide is nothing more than a string of amino acids that is similar to, but not identical to, a protein. To understand what a peptide is and how it differs from a protein, it is necessary to first understand what an amino acid is.

What Are Amino Acids?

Amino acids are biologically important molecules, but not all of them are used by living organisms. In fact, the human body requires only 20 different amino acids to function (the case for almost all living things), even though nearly 500 have been identified in the universe so far. Amino acids have two specific chemical structures, called amine and carboxylic acid groups, at opposite ends. These structures endow amino acids with a common set of functions and define how they interact with one another and with other molecules.

Trends in Peptide

Research As the ability to synthesize synthetic peptides has grown over the decades since the 1920s, something interesting has happened. Science has slowly but surely moved away from simply trying to mimic the structure of natural peptides, a practice which necessarily limited development to shorter peptides, and has instead focused on developing novel peptides that act on receptors of interest even if they bear no resemblance to native peptides.Trend in peptide length by decade:

Source: Science Direct

On average, the development time for a peptide is about 9.4 years and there are often setbacks along the way. Sometimes, peptides that are rejected as unsuitable for use get a second chance when they are altered, combined with other peptides, or applied in a new setting. As the catalog of therapeutic peptides has grown, so too has the research grown with it. For instance, the rate of discovery of peptide-addressable targets for which no peptide has yet been discovered or developed has helped to spur a frenzy of research activity. For instance, development of a melanocortin 4 receptor (MC4R) agonist could be critical in the fight against obesity and is of intense research focus. Scientists have identified the receptor, now they are searching for a peptide that is specific for it. Additionally, peptide drug delivery techniques are constantly being advanced, making it possible for peptides that were once unstable, difficult to store, or complicated to administer to become more attractive as potential therapeutics.

The peptide categories discussed below are among the most hotly researched in the world. They contain peptides that have long been used in the clinical setting as well as peptides that are under active research. This is hardly an exhaustive list though. It is just a teaser to introduce the world of peptides research.

What Are Peptides?

Peptides and proteins are both made up of amino acids that are linked together (by peptide bonds, hence the name) in long chains called polymers. The only thing that separates peptides from proteins is how big they are. While there is no absolute cutoff, peptides are made up of fewer amino acids than proteins and hence are much smaller. In general, any amino acid chain that is longer than fifty residues in length is referred to as a protein. This is because after growing beyond 50 amino acids, peptides start to fold back on themselves creating shapes and bonds that are referred to as secondary structure. Peptides are almost always linear, with minimal secondary structure (lariat loops are sometimes observed), hence the size cut off.So, peptides are smaller, simpler versions of proteins. But saying that does not do justice to the role these biochemicals play in everyday life. Research shows that peptides are primarily signaling molecules used to alter the ebb and flow of major biological systems. Peptides influence things like immune regulation, growth hormone release, extracellular matrix production, nerve cell growth and migration, and much more. Peptides are the keys to starting and stopping major biochemical cascades and, as such, are of the utmost importance to proper biological function.It’s important to remember that we consume peptides on a daily basis. Eggs, milk, beans, meat, oats, and wheat all contain peptides, proteins, and various other biologically active molecules. In addition, many popular supplements, energy drinks, and health foods are enriched with peptides that help to improve body composition, boost energy, and aid digestion. Examples of common peptides found in everyday products include collagen and creatine.

Peptide Classes

Peptides are generally divided into groupings based on their function. For instance, there are antibacterial peptides, vaccine peptides, and anticancer peptides. Unfortunately, these peptide categories often overlap, which makes strict categorization difficult and confusing. For instance, brain peptides and immune peptides often overlap. The same is true of skin peptides and immune peptides as well as skin peptides and tendon peptides. Categorizing peptides by where they are located is an untenable approach because they are often found in various tissues.

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.

Peptide Bioavailability

Peptides are short chains of amino acids that are being extensively researched for their potential therapeutic benefits. While they are commonly associated with subcutaneous (SubQ) Administration, recent advancements in peptide modification have allowed for better oral bioavailability. In fact, many peptides can now be taken orally in pill or capsule form, making them more convenient and accessible to a wider range of research and clinical studies.For example, Thymosin Beta4 (TB500) is a peptide that has been shown to have several therapeutic benefits, such as improving wound healing and reducing inflammation. In its original form, TB500 had to be administration subcutaneously to be effective. However, a newer fragment of TB500 called Thymosin Beta4 Fragment SDKP has been modified to have better oral bioavailability, meaning it can be taken orally and still produce the same therapeutic effects.Another example is BPC157, a peptide that has been shown to promote healing and reduce inflammation. In its original form, BPC157 was administered subcutaneously. However, a newer version of BPC157 that uses the Arginate salt instead of the usual Acetate salt has been shown to have better oral bioavailability, making it easier to administer.In this blog post, we’ll explore the benefits of oral peptide administration and the various modifications that have made it possible. We’ll also examine some of the misconceptions surrounding peptide administration, such as the belief that subcutaneous administration is the only effective way to administer peptides. By the end of this post, you’ll have a better understanding of the potential benefits of oral peptide administration and the different options available to you.