Education

What is Nutraceutical ?

Nutraceutical Products are derived from food sources to treat the root causes of disease ( ie chronic disease & autoimmune dysfunction ) to restore a healthy function to the total body. 

Our differences !

All of our products are formulated with the highest bioavailability. To ensure the relative absorption of a nutrient; to yield the highest therapeutic value with the lowest side-effect profile.

Bioavailability in regards to nutraceutical formulation can have a major impact on its therapeutic action.

The key stage of nutraceutical bioefficiency is oral bioavailability, which involves the following processes: the release of nutraceuticals from food matrices or nanocarriers in gastrointestinal fluids, is the solubilization of nutraceuticals and their interaction with other components of gastrointestinal fluids.

What Is Nutrient Bioavailability?

When we consume a vitamin or mineral, its bioavailability refers to the amount of the nutrient that has an active effect within our bodies. Put simply, the higher a nutrient's bioavailability is, the more of it that will get sent to the parts of the body that need it.

Here are a few examples on how to maximize bioavailability with supplements.

1. Take calcium with vitamin D***
2. Take iron an hour before a meal.
3. Combine magnesium with carbs.
4. Eat black pepper with turmeric
5. Ingest vitamin B12 in the morning.
6. Take zinc with protein.
7. Take vitamin C on an empty stomach.

***In 1975, Robert Badeen B-2-H formulator. A pioneer in functional research, working with a group of researchers at the University of Oklahoma, proved vitamin D3 is needed to take calcium across the G.I.gut*.

FYI: Surprisingly 81 percent of people take at least one medication a day. We spend more money than any other country on healthcare, yet our life expectancy is shortened, obesity is more widespread, and the rate of maternal infant death is higher than any other industrialized nation in the world. Why should we have to choose between modern medicine and getting healthy!

What is Functional Medicine ?

Functional medicine asks how and why illness occurs and restores health by addressing the root causes of disease for each individual. It is an approach to patient care that views health and illness as a part of a continuum in which all components of the human biological system interact dynamically with the environment, producing patterns and effects that change over time.

Functional medicine may be described as the clinical application of systems biology. Chronic disease is usually preceded by a period of declining function in one or more of the body’s systems.Restoration of health requires improving the specific dysfunctions that have contributed to the disease state. Functional medicine provides tools and a reproducible method to enable clinicians to identify dysfunction and promote balance in physiology as the primary means of improving patient health.

Human biology is far more complex than the human genome. In fact, most diseases are not genetically determined. It is gene expression rather than genetic inheritance that is essential in the emergence of disease. Gene expression is altered by myriad influences, including environment, lifestyle, diet, activity patterns, psycho-social-spiritual factors, and STRESS. Diet and lifestyle choices and environmental exposures can render disease more or less likely by turning on——or off——established genes.

Functional medicine directly addresses modulators of gene expression, an individual’s environment, and other underlying causes of disease through a systems-oriented approach.

Intro to Peptides

What is a Peptide?

A peptide is a biologically occurring chemical compound containing two or more amino acids connected by peptide bonds. A peptide bond is a covalent bond that is formed between two amino acids when a carboxyl group or C-terminus of one amino acid reacts with the amino group or N-terminus of another amino acid in a condensation reaction (a molecule of water is released during the reaction). The resulting bond is a CO-NH bond and forms a peptide or amide molecule. Likewise, peptide bonds are amide bonds.

The word “peptide” itself comes from πέσσειν, the Greek word meaning “to digest.” Peptides are an essential part of nature and biochemistry, and thousands of peptides occur naturally in the human body and animals. In addition, new peptides are being discovered and synthesized regularly in the laboratory as well. Indeed, this discovery and innovation in the study of peptides holds great promise for the future in the fields of health and pharmaceutical development.

How Are Peptides Formed?

Peptides are formed both naturally within the body and synthetically in the laboratory. The body manufactures some peptides organically, such as ribosomal and non-ribosomal peptides. In the laboratory, modern peptide synthesis processes can create a virtually boundless number of peptides using peptide synthesis techniques like liquid phase peptide synthesis or solid phase peptide synthesis. While liquid-phase peptide synthesis has some advantages, solid-phase peptide synthesis is the standard peptide synthesis process used today. The first synthetic peptide was discovered in 1901 by Emil Fischer in collaboration with Ernest Fourneau. Oxytocin, the first polypeptide, was synthesized in 1953 by Vincent du Vigneaud.

Peptide Terminology

Peptides are generally classified according to the amount of amino acids contained within them. The shortest peptide, one composed of just two amino acids, is termed a “dipeptide.” Likewise, a peptide with 3 amino acids is referred to as a “tripeptide.” Oligopeptides refer to shorter peptides made up of relatively small numbers of amino acids, generally less than ten. Polypeptides, conversely, are typically composed of more than at least ten amino acids. Much larger peptides (those composed of more than 40-50 amino acids) are generally referred to as proteins.

While the number of amino acids contained is a main determinate when it comes to differentiating between peptides and proteins, exceptions are sometimes made. For example, certain longer peptides have been considered proteins (like amyloid beta), and certain smaller proteins are referred to as peptides in some cases (such as insulin). For more information about the similarities and differences among peptides and proteins, read our Peptides Vs. Proteins page.

Classification of Peptides

Peptides are generally divided into several classes. These classes vary with how the peptides themselves are produced. For example, ribosomal peptides are produced from the translation of mRNA. Ribosomal peptides often function as hormones and signalling molecules in organisms. These can include tachykinin peptides, vasoactive intestinal peptides, opioid peptides, pancreatic peptides, and calcitonin peptides. Antibiotics like microcins are ribosomal peptides produced by certain organisms. Ribosomal peptides often go through the process of proteolysis (the breakdown of proteins into smaller peptides or amino acids) to reach the mature form.

Conversely, nonribosomal peptides are produced by peptide-specific enzymes, not by the ribosome (as in ribosomal peptides). Nonribosomal peptides are frequently cyclic rather than linear, although linear nonribosomal peptides can often occur. Nonribosomal peptides can develop extremely intricate cyclic structures. Nonribosomal peptides frequently appear in plants, fungi, and one-celled organisms. Glutathione, a key part of antioxidant defence in aerobic organisms, is the most common nonribosomal peptide.

Milk peptides in organisms are formed from milk proteins. They can be produced by enzymatic breakdown by digestive enzymes or by the proteinases formed by lactobacilli during the fermentation of milk. Additionally, peptones are peptides derived from animal milk or meat that have been digested by proteolytic digestion. Peptones are often used in the laboratory as nutrients for growing fungi and bacteria.

Peptide fragments, moreover, are most commonly found as the products of enzymatic degradation performed in the laboratory on a controlled sample. However, peptide fragments can also occur naturally as a result of degradation by natural effects.

Important Peptide Terms

Some basic peptide-related terms are key to a general understanding of peptides, peptide synthesis, and the use of peptides for research and experimentation:

Amino Acids – Peptides are composed of amino acids. An amino acid is any molecule that contains both amine and carboxyl functional groups. Alpha-amino acids are the building blocks from which peptides are constructed.

Cyclic Peptides – A cyclic peptide is a peptide in which the amino acid sequence forms a ring structure instead of a straight chain. Examples of cyclic peptides include melanotan-2 and PT-141 (Bremelanotide).

Peptide Sequence – The peptide sequence is simply the order in which amino acid residues are connected by peptide bonds in the peptide.

Peptide Bond – A peptide bond is a covalent bond that is formed between two amino acids when a carboxyl group of one amino acid reacts with the amino group of another amino acid. This reaction is a condensation reaction (a molecule of water is released during the reaction).

Peptide Mapping – Peptide mapping is a process that can be used to validate or discover the amino acid sequence of specific peptides or proteins. Peptide mapping methods can accomplish this by breaking up the peptide or protein with enzymes and examining the resulting pattern of their amino acid or nucleotide base sequences.

Peptide Mimetics – A peptide mimetic is a molecule that biologically mimics active ligands of hormones, cytokines, enzyme substrates, viruses or other bio-molecules. Peptide mimetics can be natural peptides, synthetically modified peptide, or any other molecule that performs the aforementioned function.

Peptide Fingerprint – A peptide fingerprint is a chromatographic pattern of the peptide. A peptide fingerprint is produced by partially hydrolyzing the peptide, which breaks up the peptide into fragments, and then 2-D mapping those resulting fragments.

Peptide Library – A peptide library is composed of a large number of peptides that contain a systematic combination of amino acids. Peptide libraries are often utilized in the study of proteins for biochemical and pharmaceutical purposes. Solid-phase peptide synthesis is the most frequent peptide synthesis technique used to prepare peptide libraries.

Peptides vs Proteins

What are the Differences?

Peptides and proteins, while similar in many regards, have several key differences that are important to understand. Oftentimes, the terms “peptide” and “protein” are used synonymously, but differing characteristics and biological activities between the two compounds prevent the terms from being interchangeable. To fully appreciate the differences between proteins and peptides, it is important to understand amino acids, the building blocks of both, and how all three (amino acids, peptides, and proteins) relate to one another.

Amino Acids

Amino acids are small but biologically vital compounds containing an amino group (NH2) and a carboxylic acid group (COOH) as well as a side-chain structure that varies between different amino acids. While hundreds of amino acids are known, only twenty are genetically combined into peptides (such as arginine, lysine, and glutamine), while others can be combined synthetically.

Importantly, amino acids make up the building blocks of peptides. When amine and carboxylic acid functional groups in amino acids join to form amide bonds, a peptide is formed. Combining two or more amino acids, whether naturally or synthetically, results in the formation of a peptide. The shortest peptide, containing two amino acids, can be referred to as a “dipeptide.” A peptide three amino acids in length is a “tripeptide,” and so on.

Peptides

Peptides are short chains of amino acids that have been linked by amide, or peptide, bonds. While the term “peptide” generally refers to a compound made up of two or more amino acids, peptides can be further classified as oligopeptides and polypeptides. Meaning “few,” “oligo” denotes that oligopeptides are made up of relatively small numbers of amino acids, generally less than ten. Polypeptides, on the other hand, are composed of more than ten amino acids.

Polypeptides and Proteins

Scientists commonly differentiate between proteins and polypeptides based on their size and structure. Regarding size, a polypeptide composed of more than 50 amino acids is generally classified as a protein, though the minimum categorization threshold can range from around 40-100 amino acids. However, 50 is a general guideline.

Secondly, proteins and polypeptides tend to differ regarding their structure. Typically, polypeptides shorter than about 40-50 amino acids in length do not fold into a fixed structure. Proteins, however, can fold into a three-dimensional, stable, fixed structure. Proteins tend to have a fixed structure for a certain function (i.e. hemoglobin, a protein responsible for transporting oxygen in the blood). Polypeptides shorter than 40-50 amino acids, on the other hand, generally do not have enough cooperative interactions to form a stable native structure.

Peptide Purity

How is Peptide Purity Achieved and Verified?

We provide peptides that exceed 99% purity. Using state-of-the-art solutions and solid-phase peptide synthetic technology, We are able to offer the finest quality peptides and proteins fit for any research study or application. Peptide purity is achieved and verified through uncompromising manufacturing and production processes, quality control measures, and the implementation of both high-performance liquid chromatography and mass spectrometry analysis.

Peptide Solubility

What Factors Determine Peptide Solubility?

Occasionally, one of the more difficult aspects of conducting research with synthetic peptides can be determining the most effective solvent in which to dissolve the peptide. Many peptides dissolve easily in aqueous solutions (sterile water), but some researchers may encounter problems related to low solubility or even insolubility, particularly when working with peptides that contain long sequences of hydrophobic amino acids. However, researchers can predict any one peptide’s solubility by studying the known characteristics of its amino acids.

A peptide’s solubility is mainly determined by the physical properties of its amino acids. Amino acids can be classified as basic, acidic, polar uncharged, or non-polar. Non-polar amino acids are hydrophobic (they do not dissolve in aqueous solutions). Peptides containing a relatively large number of non-polar amino acids or polar uncharged amino acids generally dissolve more effectively in organic solvents such as DMSO, propanol, isopropanol, methanol, or DMF. Peptides with a high content of acidic amino acids can typically be dissolved in basic solvents (such as ammonium hydroxide, although this should not be used with peptides containing Cys), and, conversely, peptides containing a relatively high number of basic amino acids can generally be dissolved effectively in acidic solvents (such as acetic acid solution). However, researchers should always attempt to dissolve peptides in sterile water first, especially when the peptide contains less than five residues (amino acids), as these peptides generally dissolve quite easily in water.