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Collagen  is  the largest and most abundant protein in the body  (our skin is made up of 95% collagen)  and  such as it is a key buildingblock  for everything from  connective tissues of vital organs (heart,lungs,etc.),joints, ligaments and tendons, to hairs, nails and the dermis layer of our skin.

Collagen contains specific amino acids : Glycine, Proline, Hydroxyproline and Arginine. 

Collagen food supplement is proven to provide our body with amino acids, that necessary to support collagen production in order to remain active-healthy body and youthful-looking skin.



Collagen is an anti-aging essential that maintain tissue suppleness and elasticity to keep youthful appearance. Clinical studies confirm the efficacy of collagen. Fish collagen peptides have been studied extensively for many years in Japan.





Most of us were born with abundant supply of collagen. As babies, our skin was plump, firm and smooth.  Unfortunately, as we aged, our body loses ability to produce collagen  and hyaluronic acid plateaus in our mid to late 20.

Starting around age 30, those first fine lines and wrinkles appears on our face. And it's go downhill from there, lose about 1-2% of our collagen yearly.

With age, collagen production slows and the cells structures weaken.   The skin gets thinner and is easier to damage, hair gets lifeless, skin sags and wrinkles,  tendons and  ligaments become less elastic, joints get stiff etc.










Skin is the mirror of our inner health.  As we age our skin starts loosing collagen and elastin, leading to signs of ageing which include the following:


Fine Line and Wrinkles:

As we age our skin starts showing fine lines these are the lines that occur around our mouth, face, eyes, nose and forehead which are folded or ridged.  These visible lines are called wrinkles. Wrinkles can occur anywhere on the face. They are not like fine lines, but much deeper that starts appearing as you get older.


Dry Skin:

Your skin is protected by its own natural oils, when you wash your skin with soap the oils are washed away too and the skin becomes dry, itchy and flaky. Older skin has fewer sweat glands and oil glands, which makes the skin more prone to conditions related to dryness, roughness and itching.


Dull Skin/ Glow-less:

There are various factors that make your skin appear dull. Extreme wind, temperature and air condition causes the skin to flake, chap and feel tight. Lipid part present under the skin becomes oxidized and makes your skin dull and yellow which appears glow less


Dark Spots:

Dark patches or age spots which come very gradually over years are round but often with irregular borders. Melanocytes tends to increase in number and cluster in some areas forming a dark spot. These dark spots are formed when the skin is exposed more to sun resulting in sun burns. This darkens the skin and leads to dark spots on skin.


Sagging Skin / Lose Skin:

Sagging is nothing but loosening and drooping of skin with age. Collagen the main supporting structure of skin, which decreases in content with age and skin becomes dull and stretched.  Loss of volume on cheeks, around the eyes becomes clearly visible leading to sagging under eyes. Too much muscular action can also lead to loose skin.


Open Pores:

Pores are the small openings on the skin. Open pores allows lot of dust and other microorganism to enter the skin which may lead to acne, oily skin and many allergic reactions of skin. Open pores enlarge when they become clogged with dirt, oil or bacteria causing irritation redness and may leads to acne and other skin diseases.


Patchy skin:

Patchy skin has uneven skin complexion. Uneven skin complexion can cause hyper pigmentation where too much melanin is produced in the body. Patchy skin is caused by the pigmentation of skin cells called melanoma, density, blood vessels changes or growth of foreign organisms on the skin.


Broken blood vessels:

There is a higher risk of Blood vessel rupture in older and thinner skin that are likely to break and get damaged. They may also enlarge.



  • Genetics:

Cellular aging is a process where the cell becomes old and no longer replicates. Cellular aging leads to DNA damage, decrease cellular replication, reduce the regeneration capacity of tissue stem cells, and accumulation of metabolic damage.  Skin cells are one of the most rapidly dividing cells in the body. At the end of the chromosomes there are stretches of DNA called telomeres.  Every time the cell divides, the DNA has to be copied due to which telomeres reduce in size. Because of this telomere shortening it will not divide further, it becomes inactive or senescent. This shortening process is one of the main factors that is associated with aging.

  • Hormones:

The sex hormones have greater influence on the skin than any other hormone. One of the most important factors involved in the intimation of ageing is the endocrine system. Endocrine system produces and regulates hormones. Along with age, the endocrine system produces lower levels of hormones. The reduction of these hormones is believed to increase skin thickens, dryness, and loss of elasticity.

  • Environmental Factors:

Repeated sun exposure is the primary cause of premature ageing. UV rays damages the skin fibers elastin. It causes the skin to sag and lose its ability to snap back after stretching.UV rays falls on skin and damages DNA in skin cells that leads to skin diseases including premature ageing, and other inflammatory conditions.  


  • Cigarette smoking:

Cigarette smoke can cause skin cracks and wrinkles because it reduces the levels of nitric oxide (cellular gas). Tobacco smoke leads to accumulation of free radicals which results in DNA damage, making skin more prone to diseases and ageing. Smokers tend to have more wrinkles, uneven tone, and dehydrated, dull and weak skin than non-smokers.

  • Alcohol:

Drinking too much alcohol leads to rosacea, the condition where the skin becomes red with small blisters on cheeks and nose. The metabolism of alcohol is molecules known as aldehydes which cause damage to the cells.  Alcohol causes dehydration and also makes the skin more prone to fine lines and wrinkles.



Collagen peptide is hydrolyzed collagen (gelatin) degraded with proteolytic enzyme or under acidic conditions, retaining almost all of its original amino acid composition.   Much different from other protein sources, collagen peptides contain a unique combination and ratio of amino acids (protein), most importantly, glycine, proline, hydroxyproline and arginine.

Diet, age, stress, digestive system and physical activity all affect our ability to provide the body with the nutritional raw materials it requires to properly support joint and connective tissue health. Collagen should be an essential nutritional component for those wanting to remain healthy and active throughout their life.





Our collagen peptides extracted through a complex PATENTED hydrolysis process. To provide the highest quality possible, we produce collagen type I extracted from fish, presenting unmatched advantages. Our Collagen is free from risk of animal diseases or pathogens such as Bovine Spongiforms Encephalopathy (BSE).

Fish collagen peptides have been shown to possess antioxidant activity and improve water-absorbing and water-holding capacity. It has also been known to effectively repress skin damage caused by UVB rays and help maintain skin smoothness.

Type I Fish Collagen is the most abundant of the many types of Collagen and are found in bones, tendons, skin and tissues. Studies support that collagen peptides type I extracted from fish consist of small peptide molecules that have a superior bioavailability and digestibility compare to other collagen products.

Due to smaller molecular weight, it is absorbed at a higher level through the intestinal barrier into the bloodstream and carried throughout the body, leading to the collagen synthesis in the joint tissues, bones and skin dermis.



In nature, collagen is found exclusively in animals, especially in the flesh and connective tissues of mammals. Collagen is a part of the connective tissue that in the skin helps in firmness, suppleness and constant renewal of skin cells. Collagen is vital for skin elasticity.

Ligaments are another type of connective tissue that attach two bones and consequently hold the joints together. Tendons are similar but different type of tissue that attached the muscles to the bones. All of these tissues, the bones, ligaments, tendons and the skeletal muscles themselves, are made up of proteins. One of the most predominant proteins is called collagen.

Collagen is the main component of connective tissue, and is the most abundant protein in mammals, making up about 25% to 35% of the whole-body protein content.



Collagen microscopically occurs in elongated fibrils. It is mostly found in fibrous tissues such as tendon, ligament and skin, and is also abundant in cornea, bone, blood vessels, cartilage, inter vertebral disc and the digestive tract.

In muscle tissue, collagen serves as a major component of endomysium. 1 to 2% of the muscles are formed of collagen and around 6% of the total weight of muscles is formed of collagen. Gelatin used in food is collagen that has been irreversibly hydrolyzed.



In the mid-1930, collagen was first discovered to have a molecular structure. Nobel laureates Crick, Pauling, Rich and Yonath and others including Brodsky, Berman, and Ramachandran have been researching the structure of collagen and their possible functions.

After several speculations of individual peptide chain, the final model that has been developed is the "Madras" model which provided an essentially correct model of the molecule's quaternary structure although this model still required some refinement. It is a triple-helical structure.

Collagen is further packed into fibrillar collagen types with hexagional or quasi hexagonal shapes. The packing may be 'sheet-like' or microfibrillar. The microfibrillar structure of collagen fibrils in tendon, cornea and cartilage has been directly imaged by electron microscopy. The microfibrillar structure of adult tendon was confirmed in 2006 by Fraser, Miller and Wess (amongst others). They found the D-periodic pentameric arrangement and termed it microfibril.



Collagen contains specific amino acids : Glycine, Proline, Hydroxyproline and Arginine. These amino acids have a regular arrangement in each of the three chains of these collagen subunits. 

The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp, where X may be any of various other amino acid residues. Proline or hydroxyproline constitute about 1/6 of the total sequence. Glycine (Gly) is found at almost every third residue. Glycine accounts for 1/3 of the sequence meaning that approximately half of the collagen sequence is not glycine, proline or hydroxyproline. Proline (Pro) makes up about 17% of collagen.

In addition, the regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin. In silk 75-80% is -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 group. High glycine contents are not found in globular proteins except in very short sections of their sequence. Because glycine is the smallest amino acid with no side chain, it plays a unique role in fibrous structural proteins.  Collagen also has two uncommon derivative amino acids that are 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 co- factor.

Collagens do not contain chemically reactive side groups unlike in enzymes and transport proteins. Collagen determines cell phenotype, cell adhesion, tissue regulation and infrastructure and its non-proline rich regions have cell or matrix association/regulation roles. Left handed helices are formed because of the high content of proline and hydroxyproline rings, with their geometrically constrained carboxyl and (secondary) amino groups along with abundance of glycine. The left handed helices are formed without any intrachain hydrogen bonding.

Hydroxyproline is derived from proline and Hydroxylysine derived from lysine. Depending on the type of collagen, varying numbers of hydroxylysines are glycosylated (mostly having disaccharides attached). In addition, the regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin. In silk 75-80% is -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 group.  High glycine contents are not found in globular proteins except in very short sections of their sequence. Because glycine is the smallest amino acid with no side chain, it plays a unique role in fibrous structural proteins. Cortisol stimulates degradation of collagen into amino acids.




In type I collagen, and possibly all fibrillar collagens if not all collagens, each of the triple helices forms a right-handed super-super-coil that is referred to as the collagen microfibril.  Thereafter, each of the microfibril is interdigitated or intercalated with its neighboring microfibrils. This strengthens the structure of the individual molecules.



Individually there are three polypeptide strands. These are called alpha chains and each of them has a conformation of a left-handed helix. An alpha helix is a different structure with a right handed conformation.

Further the three left-handed helices are twisted together into a right-handed coiled coil, forming a triple helix or "super helix". The final cooperative quaternary structure stabilized by numerous hydrogen bonds.



The tensile strength of collagen depends on the formation of covalent intermolecular cross-links between the individual protein subunits. The fibril containing collagens in higher vertebrates (types I, II, III, V and XI) are cross-linked through a mechanism based on the reactions of aldehydes generated enzymically from lysine (or hydroxylysine) side-chains by lysyl oxidase. Certain other collagen types (e.g., collagen type IX of cartilage) are also cross-linked by the lysyl oxidase mechanism.



Different collagen types form larger fibrillar bundles with the help of several different classes of proteins like glycoproteins and proteoglycans. Collagen fibrils are semi-crystalline aggregates of collagen molecules. These are actually bundles of fibrils.

Each of the tissues has a different arrangement of these fibrils to give it different structure, shape and tensile strength. In bone for example, entire collagen triple helices lie in a parallel, staggered array. The gaps are 40 nm between the ends of the tropocollagen subunits. This serves as the nucleation sites for the deposition of long, hard, fine crystals of the mineral component - hydroxyapatite, Ca10(PO4)6(OH)2 with some phosphate. This turns collagen in cartilage that is softer into hard bone. Type I collagen gives bone its tensile strength.



More than 20 genetically distinct collagens exist in animal tissues. Collagen types I, II, III, V and XI self-assemble into D-periodic cross-striated fibrils. Here the D is approximately 67 nm and there is characteristic axial periodicity of collagen. These form the most abundant collagens in vertebrates.

  • Type I collagen is found throughout the body except in cartilaginous tissues. It is also synthesized in response to injury and in the fibrous nodules in fibrous diseases.
  • Type II collagen is found in cartilage, developing cornea and vitreous humour. These are formed from two or more collagens or co-polymers rather than a single type of collagen.
  • Type III collagen is found in the walls of arteries and other hollow organs and usually occurs in the same fibril with type I collagen.

Type V collagen and type XI collagen are minor components of tissue and occur as fibrils with type I and type II Type I collagen fibrils are used as the reinforcing rods in construction of bone. Certain mutations in the alpha1(I) (I) or  alpha2(I) genes lead to osteogenesis imperfecta, or brittle-bone disease. The most severe type is an autosomal dominant, lethal disease resulting in death in utero or shortly after birth. Milder forms generate a severe crippling disease. As might be expected, many cases of osteogenesis imperfectaare due to deletions of all or part of the very long alpha1(I) gene.

However, a single amino change is sufficient to cause certain forms of this disease. As we have seen, a glycine must be at every third position for the collagen triple helix to form mutations of glycine to almost any other amino acid are deleterious, producing poorly formed and unstable helices. Since the triple helix forms from the C- to the N-terminus, mutations of glycine near the C-terminus of the &alpha1(I) chain are usually more deleterious than those near the N-terminus the latter permit substantial regions of triple helix to form. Mutant unfolded collagen chains do not leave the rough ER of fibroblasts (the cells that make most of type I collagen), or they leave it slowly. As the ER becomes dilated and expanded, the secretion of other proteins (e.g., type III collagen) by these cells also is slowed down.

Because each type I collagen molecule contains two &alpha1(I) and one alpha2(I) chains, mutations in the alpha2(I) chains are much less damaging. To understand this point, consider that in a heterozygote expressing one wild-type and one mutant alpha1(I) protein 50 percent of the collagen molecules will have the abnormal alpha2(I) chain. In contrast, if the mutation is in the alpha1(I) chain, 75 percent of the collagen molecules will have one or two mutant alpha1(I) chains. In fact, even low expressionof a mutant alpha1(I) gene can be deleterious, because the mutant chains can disrupt the function of wild-type alpha1(I) chains when combined with them. To study such mutations, experimenters constructed a mutant alpha1(I) collagen gene with a glycine-to-cysteine substitution near the C-terminus.



Type I collagen is the most abundant collagen in the body.

During translation, two types of peptide chains are formed on ribosomes along the rough endoplasmic reticulum (RER). These are called the alpha-1 and alpha-2 chains. These peptide chains (known as preprocollagen) have registration peptides on each end and a signal peptide.

The pre-procollagen is then released into the lumen of the RER. Thereafter the signal peptides are cleaved inside the RER and the peptide chains are now called pro-alpha chains. Hydroxylation of lysine and proline amino acids occurs inside the lumen. This process is dependent on ascorbic acid (Vitamin C) as a cofactor. Further glycosylation of specific hydroxylysine residues occurs. Triple helical structure is formed inside the endoplasmic reticulum from each two alpha-1 chains and one alpha-2 chain. This is called procollagen.    Procollagen is transported into the golgi apparatus, where it is packaged and secreted by exocytosis.Once outside the cell, the registration peptides are cleaved and tropocollagen is formed by procollagen peptidase. These tropocollagen molecules gather to form collagen fibrils, via covalent cross-linking by lysyl oxidase which links hydroxylysine and lysine residues. Multiple collagen fibrils form into collagen fibers. Collagen may be attached to cell membranes via several types of protein, including fibronectin and integrin.

Nutricosmetics represent a potential intervention to improve beauty and health. Nutricosmetics (also known as beauty from within and oral cosmetics) refer to nutritional supplements that are taken orally to improve beauty and health, in particular the structure of the skin.

Because collagen-derived peptides have a variety of unique biological properties that have potential health benefits, they may slow the skin aging process. Schwartz and Park found that women and men who took a hydrolyzed collagen supplement for 8 weeks had significant improvements in skin dryness and fine lines /wrinkles. The women also had a significant improvement in the content of collagen in the skin dermis, with its ability to impact cellular functions, its protective qualities may prevent the alterations in the extracellular matrix of the skin that occur with aging. The functioning of the extracellular matrix has a large impact on the aging of skin, a result of fragmented collagen fibrils present in the matrix.

Collagen may specifically help reduce the intrinsic aging process (influenced by genetics), while restoring the skin and protecting it from the extrinsic (environmental) aging factors. Reactive oxygen species have been implicated in a number of age-related skin disorders.  

Because healthy skin is associated with a youthful appearance, skin satisfaction may be related to body satisfaction. For women in particular, a youthful and thin physical appearance has often been found to be related to attractiveness.Changes associated with aging such as wrinkled skin and weight gain may take women away from societal ideals of attractiveness and may result in decreased skin and body satisfaction. Due to the potential reductions in body satisfaction as a result of changes in skin aging, research is needed to examine the effects of interventions that can potentially improve skin appearance, and thereby lead to improvements in both skin satisfaction and body satisfaction.




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