Peptides 101

Peptides are fragmented components proteins. They consist of short chains of amino acids linked by amide bonds. There are biologically occurring peptides. The formation of amino acids determines which specific protein is created.
Many proteins make up the fundamental building blocks of the skin. These proteins create connective tissues, such as collagen, elastin and fibroblast. The fibers crisscross to form the dermal matrix. It is these protein formations that provide the skin with its structural support. The absence of this framework causes the skin to lose firmness and elasticity. It also changes the texture of the skin, leads to sagging and causes wrinkles to appear.

Peptides In Skincare

The skincare industry boasts incredible anti-aging effects when certain peptides are applied topically. Some of these claims are wildly exaggerated or almost completely false. However, emerging research continues to affirm the benefits of certain peptides. Studies are showing that certain peptides hold revitalizing capabilities that can help to restore the building block of dermal matrix and rejuvenate the skin.
A number of factors cause the skin to age. Thus, there is no one simple solution to reversing the signs of aging. That said, peptides can provide a significant role in daily skincare. As science continues to bare down on what specific peptides are beneficial to the health of your skin, new formulas will emerge.

Classes of Peptides

As mentioned, there are hundreds of peptides. In turn, these peptides are then organized into several classes. Determining class placement is dependent on the way that these amino acid chains are created.

Milk Peptides

Enzymatic breakdown of the milk protein called casein to create two naturally occurring milk peptides. Fermentation of milk causes the milk protein, proteinases to form lactobacilli.

Ribosomal Peptides

Translation of mRNA results in the synthetization of Ribosomal peptides. These are maturated during proteolysis and function as hormones and signaling molecules in higher organisms. Other organs create microcins which are peptides that act as an antibiotic. They are utilized strictly by ribosomes due to the translation process of amino acid residues.
That said, there are a number of these peptides that undergo modifications post-translationally. This include:
• Phosphorylation
• Hydroxylation
• Sulfonation
• Palmitoylation
• Glyocsylation
• Disulfide
Typically, these chains occur in linear patterns with some structures of the lariat variety occasionally forming. In some post-translation manipulations, more exotic formations occur in platypus venom when L-Amino Acids forms D-Amino Acids.

Non-Ribosomal Peptides

As opposed to ribosomal assembly, non-ribosomal Peptides are developed by enzymes specific to each peptide. Glutathione is the most common non-ribosomal peptides. In aerobic organisms, glutathione contributes to antioxidant defense. These peptides are found in fungi, plants and unicellular organisms. They are developed by non-ribosomal peptide synthetases by modular enzyme complexes.

Peptones

Proteolysis in animal milk and digested meat are responsible for the creation of peptones. They contain small peptides used in fats, metals, salts, vitamins and other compounds, and provide nutrients for growing fungi and bacteria.

Peptide Fragments

Source proteins are quantified and identified through the use of Peptide Fragments. These fragments are most often created in laboratories during a controlled performance of enzyme degradation. It is also used paleontological or forensic samples which have been degraded naturally.

Todd Ruggets
Todd Ruggets

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