• Helps reduce body fat
• Naturally helps increase your metabolism
• Helps promote higher energy levels
• Helps your body retain lean muscle tissue

Plus
• Promotes Better Sleep
• Supports Healthy Joint Function
• Promotes Skin, Hair and Nail Growth, and Quality

• Glycine
• Proline
• Hydroxyproline
• Arginine

These amino acids have been shown to influence weight loss, bone and connective tissue, improvements in skin appearance, optimal body growth and repair, improved metabolism, support of growth hormone levels and healing, especially wounds.

These four special amino acids also maintain lean body mass which helps provide a firm toned and more youthful looking body – as well as help improve skin elasticity and joint function.

Renovatio is the only 100% collagen supplement that is enzymatically pre-digested (hydrolyzed) to ensure rapid and maximum absorption. Health Direct breaks down the protein in a similar manner to the way your body would – with natural enzymes. Since the protein is broken down to its smallest components, your body completely absorbs it after ingestion.

No other collagen supplement on the market today is as bioavailble as Renovatio. No other collagen supplement contains more collagen per tablespoon or is more absorbable than Renovatio. Every tablespoon delivers 8 grams of enzymatically pre-digested collagen that can be rapidly used by the body to tighten and tone the muscles, increase joint function and flexibility.

If taken when dieting and at bedtime on an empty stomach, Renovatio liquid collagen supplement can help to reduce body fat.

Composition and structure

The tropocollagen or "collagen molecule" subunit is a rod about 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands, each of which is a left-handed helix, not to be confused with the commonly occurring alpha helix, which is right-handed. These three left-handed helices are twisted together into a right-handed coiled coil, a triple helix, a cooperative quaternary structure stabilized by numerous hydrogen bonds. Tropocollagen subunits spontaneously self-assemble, with regularly staggered ends, into even larger arrays in the extracellular spaces of tissues. There is some covalent crosslinking within the triple helices, and a variable amount of covalent crosslinking between tropocollagen helices, to form the different types of collagen found in different mature tissues — similar to the situation found with the α-keratins in hair. Collagen's insolubility was a barrier to study until it was found that tropocollagen from young animals can be extracted because it is not yet fully cross linked.

Collagen fibrils are collagen molecules packed into an organized overlapping bundle. Collagen fibers are bundles of fibrils.

A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-X-Pro or Gly-X-Hyp, where X may be any of various other amino acid residues. Gly-Pro-Hyp occurs frequently. This kind of regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin. 75-80% of silk is (approximately) -Gly-Ala-Gly-Ala- with 10% serine — and elastin is rich in glycine, proline, and alanine (Ala), whose side group is a small, inert methyl. Such high glycine and regular repetitions are never found in globular proteins. Chemically-reactive side groups are not needed in structural proteins as they are in enzymes and transport proteins. The high content of Pro and Hyp rings, with their geometrically constrained carboxyl and (secondary) amino groups, accounts for the tendency of the individual polypeptide strands to form left-handed helices spontaneously, without any intrachain hydrogen bonding.

Because glycine is the smallest amino acid, it plays a unique role in fibrous structural proteins. In collagen, Gly is required at every third position because the assembly of the triple helix puts this residue at the interior (axis) of the helix, where there is no space for a larger side group than glycine’s single hydrogen atom. For the same reason, the rings of the Pro and Hyp must point outward. These two amino acids thermally stabilize the triple helix — Hyp even more so than Pro — and less of them is required in animals such as fish, whose body temperatures are low.

In bone, entire collagen triple helices lie in a parallel, staggered array. 40 nm gaps between the ends of the tropocollagen subunits probably serve as nucleation sites for the deposition of long, hard, fine crystals of the mineral component, which is (approximately) hydroxyapatite, Ca₅(PO₄)₃(OH), with some phosphate. It is in this way that certain kinds of cartilage turn into bone. Collagen gives bone its elasticity and contributes to fracture resistance.

Types of collagen and associated disorders

Collagen occurs in many places throughout the body. There are 28 types of collagen described in literature.

Collagen diseases commonly arise from genetic defects that affect the biosynthesis, assembly, posttranslational modification, secretion, or other processes in the normal production of collagen.

Synthesis

Amino acids

Collagen has an unusual amino acid composition and sequence:

• Glycine (Gly) is found at almost every third residue
• Proline (Pro) makes up about 9% of collagen
• Collagen contains two uncommon derivative amino acids not directly inserted during translation. These amino acids are found at specific locations relative to glycine and are modified post-translationally by different enzymes, both of which require vitamin C as a cofactor.
• Hydroxyproline (Hyp), derived from proline.
• Hydroxylysine, derived from lysine. Depending on the type of collagen, varying numbers of hydroxylysines have disaccharides attached to them.

Collagen I formation

Most collagen forms in a similar manner, but the following process is typical for type I:

1. Inside the cell
1. Three peptide chains are formed (2 alpha-1 and 1 alpha-2 chain) in ribosomes along the Rough Endoplasmic Reticulum (RER). These peptide chains (known as preprocollagen) have registration peptides on each end; and a signal peptide is also attached to each
2. Peptide chains are sent into the lumen of the RER
3. Signal Peptides are cleaved inside the RER and the chains are now known as procollagen
4. Hydroxylation of lysine and proline amino acids occurs inside the lumen. This process is dependent on Ascorbic Acid (Vitamin C) as a cofactor
5. Glycosylation of specific hydroxylated amino acid occurs
6. Triple helical structure is formed inside the RER
7. Procollagen is shipped to the golgi apparatus, where it is packaged and secreted by exocytosis
2. Outside the cell
1. Registration peptides are cleaved and tropocollagen is formed by procollagen peptidase.
2. Multiple tropocollagen molecules form collagen fibrils, and multiple collagen fibrils form into collagen fibers
3. Collagen is attached to cell membranes via several types of protein, including fibronectin and integrin.

Synthetic pathogenesis

Vitamin C deficiency causes scurvy, a serious and painful disease in which defective collagen prevents the formation of strong connective tissue. Gums deteriorate and bleed, with loss of teeth; skin discolors, and wounds do not heal. Prior to the eighteenth century, this condition was notorious among long duration military, particularly naval, expeditions during which participants were deprived of foods containing Vitamin C. In the human body, a malfunction of the immune system, called an autoimmune disease, results in an immune response in which healthy collagen fibers are systematically destroyed with inflammation of surrounding tissues. The resulting disease processes are called Lupus erythematosus, and rheumatoid arthritis, or collagen tissue disorders.

Many bacteria and viruses have virulence factors which destroy collagen or interfere with its production.

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