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The science behind Pure GOLD COLLAGEN®

MINERVA Research Labs brings you Pure GOLD COLLAGEN®, the new generation skincare solution based on a formula specifically developed to offer a unique blend of collagen and active ingredients for high absorption and bioavailability.


MINERVA Research Labs collaborates with the University of Oxford, University of Portsmouth, several dermatologists, aesthetic medicine and skin specialists, and works according to ISO 9001 quality standards. MINERVA Research Labs is committed to ensuring only the highest quality food ingredients are sourced from partners such as Rousselot SAS of France, with whom it has a strategic alliance, Polaris in France and Lipoid in Germany. MINERVA Research Labs understands the complex science behind collagen and how ageing affects the skin in order to develop and deliver innovative and effective solutions to the consumer.

Please explore this section to understand the science and research behind Pure GOLD COLLAGEN®...              

What is Collagen?

THE COLLAGEN MOLECULE Collagen is the main structural protein of the different connective tissues present in animals. It is mostly found in fibrous tissues, such as tendons and ligaments, and is also abundant in corneas, cartilage, bones, blood vessels, the gut, and intervertebral discs. Collagen is the major insoluble fibrous protein found in the extracellular matrix of the skin, together with elastin and hyaluronic acid. The collagen family consists of 28 different proteins 1,2, which account for 25% - 35% of the total protein mass in mammals and play a pivotal role in the structure of several tissues, such as skin and bones, providing rigidity and integrity 3,4. In fact, collagens are the major structural element of all connective tissues and the most abundant proteins in the animal kingdom. The extracellular matrix (ECM) of connective tissues is formed by diverse protein families, involved in the structural integrity and several physiological functions. Composition and structure of the ECM vary considerably in the different types of connective tissues and result in unique functional and biological characteristics 5. The five most common types of collagen are:

  • Type I: dermis, tendon, ligaments and bone
  • Type II: cartilage, vitreous body, nucleus pulposus
  • Type III: skin, vessel wall, reticular fibres of most tissues (lungs, liver, spleen …)
  • Type IV: forms the basal lamina, the epithelium-secreted layer of the basement membranes
  • Type V: lung, cornea, hair and fetal membranes

Based on their structure and three-dimensional organization, they can be grouped into fibril-forming collagens, fibril-associated collagens (FACIT), network-forming collagens, anchoring fibrils, transmembrane collagens (MACIT), basement membrane collagens and others with unique functions (Tab. 1) 2,5. In the human body 80 – 90% of the total collagen consists of the fibril-forming collagens. Types I and V collagens contribute to the structure of the bone, while type II and XI collagen fibrils are involved in the formation of the fibrillar matrix in the articular cartilage 5-7. Type IV collagen, in contrast, forms a two-dimensional reticulum and this more flexible triple helix is restricted to basement membranes 5,13.

Fibrils-forming collagens  
I Dermis, tendon, ligaments, bone, cornea
II Cartilage, vitreous body, nucleus pulposus
III Skin, vessel wall, reticular fibres of most tissues (lungs, liver, spleen, etc.)
V Lung, cornea, bone, fetal membranes (together with type I collagen)
XI Cartilage, vitreous body
Basement membrane collagens  
IV Basement membranes
Microfibrillar collagen  
VI Widespread: dermis, cartilage, placenta, lungs, vessel wall, intervertebral disc
Anchoring fibrils  
VII Skin, dermal-epidermal junctions, oral mucosa, cervix
Hexagonal network-forming collagens  
VIII Endothelial cells, Descemet’s membrane
X Hypertrophic cartilage
Fibrils-associated collagens (FACIT)  
IX Cartilage, Vitreous humor, cornea
XII Perichondrium, ligaments, tendon
XIV Dermis, tendon, vessel wall, placenta, lungs, liver
XIX Human rhabdomyosarcoma
XX Corneal epithelium, embryonic skin, sternal cartilage, tendon
XXI Blood vessel wall
Transmembrane collagens (MACIT)  
XIII Epidermis, hair follicle, endomysium, intestine, chondrocytes, lungs, liver
XVII Dermal-epidermal junctions
XV Fibroblasts, smooth muscle cells, kidney, pancreas
XVI Fibroblasts, amnion, keratinocytes
XVIII Lungs, liver

Tab 1. Tissue distribution of the different collagen molecules.

(Adapted from ref. 5 and 8) Collagens are secreted mainly by fibroblasts in the connective tissues 2, but also numerous epithelial cells make certain types of collagens. The different collagens and structure they form have the purpose to help tissues resist stretching. Fibroblasts are sensitive to physical and chemical stimuli, which can induce both fibroblasts activation and proliferation. The activation of fibroblasts results in an increase in the production of collagen.


Despite the high structural diversity among the different collagen types, all collagen molecules share a triple-stranded helical structure composed of three polypeptide chains (α-chains) and pack together to form long thin fibrils arranged in bundles 4,5. The triple-helical structure is characterized by containing domains with an abundance of three amino acids: glycine, proline and hydroxyproline (Figure 1), that form the characteristic repeating motif Gly-X-Y, where X and Y can be any amino acid, but usually these positions are occupied by proline and hydroxyproline 5,13. The presence of a glycine residue, the smallest amino acid, in every third position of the polypeptide chains is essential for the assembly into a triple helix. Each amino acid has a particular function. A variety of unique properties are due mainly to additional protein domains that interrupt the triple helix, forming other kinds of three-dimensional structures{Gelse, 2003 #41} 5,13. The helix-forming repeated motif (Gly-X-Y) is the fundamental structure unit in fibril-forming collagens (type I, II and III) and it results in triple helical domains of 300 nm in length and with a diameter of 1.5 nm. Each chain contains about 1000 amino acids wound around one another in a characteristic right-handed triple helix, that consists of 3 coiled subunits 5,13 (Figure 2). For example, two α1 chains and one α2 chain constitute type I collagen. Native triple helices are characterized by their resistance to proteases, such as pepsin or trypsin 9 and can only be degraded by specific collagenases (metalloproteinases) 5. Skin

Figure 2. Triple-stranded helical structure of the collagen fibrils.

Multiple triple helices form a collagen fibril and multiple fibrils pack together to form a collagen fibre. Generally collagen fibrils are made of different collagen types: for example, collagen I and III in the skin, collagen II and III in cartilage 4. In the classical fibril-forming collagens (types I, II, III, V, XI, XXIV and XXVII), many collagen molecules pack together side-by-side, forming fibrils with a diameter of 24 and 400 nm. In fibrils, adjacent collagen molecules are displaced from one another by about 70 nm. This staggered arrangement of individual collagen monomers produces a striated effect that can be seen in the electron microscope. The unique properties of the fibrous collagens are due to the ability of the triple helices to form such side-by-side interactions 5,13. Short segments at either end of the collagen chains (C-terminus and N-terminus) are important in the formation of collagen fibrils. The C-propeptide has a fundamental role in the initiation of triple helix formation, whereas the N-propeptide is involved in the regulation of primary fibril diameters 5 (Figure 3). These segments (telopeptides) do not have a triple-helical conformation and contain the amino acid hydroxylysine. The side-by-side interaction of collagen molecules are stabilized by covalent cross-links that form between two lysine (or hydroxylysine) residues at the C-terminus of one collagen molecule with two similar residues at the N-terminus of an adjacent molecule. These cross-links stabilize the structure of collagen molecules and generate a strong fibril 13.


Collagen synthesis and assembly follows the normal pathway for a secreted protein (Figure 4). The activation of fibroblasts in the connective tissues results in an increase in the production of collagen. The mechanism of collagen formation is well known. The genetic information encoded in the DNA is “read” (transcription process in the nucleus), the mature mRNA is then transported to the cytoplasm and “translated” (translation process) to produce the single polypeptide chains (α-chains) at the rough endoplasmatic reticulum (ER) 5. Each α-chain has a terminal peptide sequence, also known as trimerization domain, which drives the assembly of the longer precursors, which are termed procollagens 4.


Figure 4. Schematic overview of the collagen synthesis.

Ribosome-bound mRNA is translated into growing preprocollagen molecules that are assembled inside the fibroblasts, into the lumen of the ER 5,4,13. In the ER, the procollagen chain undergoes a series of posttranslational modifications, as with other secreted proteins. First, glycosylation of procollagen occurs in the rough ER and Golgi complex. In addition, specific proline and lysine residues in the middle of the chains are hydroxylated by membrane-bound hydroxylases. Lastly intra-chain disulphide bonds between the N- and C- propeptide sequences align the three chains before the triple helix forms in the ER. The formation of triple helices is preceded by the alignment of the C-terminal domains of three α-chains and initiates the formation of the triple helix progressing to the N-terminus 5,13 (Figure 5). After procollagen is processed and assembled, the triple-helical molecules are packaged within the Golgi compartment into secretory vesicles and released into the extracellular space 5. Finally the N-terminal and C-terminal propeptides are cleaved by extracellular enzymes (procollagen peptidases). The resulting protein, often called tropocollagen, consists almost entirely of a triple stranded helix. Excision of both propeptides allows the collagen molecules to polymerise and spontaneously assembly into normal fibrils in the extracellular space (Figure 5). Defects in this process have serious consequences. The stability and the function of collagen are also determined by the formation of covalent cross-links, which contribute to a stable network formation 5,4,13.


The formed fibrils can be oriented differently in distinct types of tissues. In tendons, the type I collagen fibrils align parallel to each other and form bundles or fibres, whereas in the skin, the orientation is more randomly with the formation of a complex network of interlaced fibrils 5. Collagens differ in their ability to form fibrils and fibres and to organize these structures into networks. For example, type II is the characteristic and predominant component in cartilage. Its fibrils are smaller in diameter than type I (15 – 50 nm) and are oriented randomly in the viscous proteoglycan matrix. Such rigid macromolecules impart a strength and compressibility to the matrix and allow it to resist large deformations in shape. This property allows joints to absorb shocks 13. Type II collagen chains are cross-linked to proteoglycans in the matrix by type IX collagen (fibril-associated collagens) in cartilage and the vitreous body 5. Type IX collagen is characterized by long triple helices interrupted by short non-helical and flexible domains. The globular N-terminal domain extends from the fibrils and these protruding are thought to anchor the fibrils to proteoglycans and other components of the extracellular matrix 5,13 (Figure 6). Type VI collagen has an unusual structure: the molecule is formed by three different α-chains (α1, α2 and α3) with short triple-helical regions about 60 nm long separated by rather extended globular domains about 40 nm long 5. Fibrils of pure type VI collagen look like beads on a string. In many connective tissues, type VI collagen is bound to type I fibrils to form thicker collagen fibres 13 (Figure 6). In some places, several extracellular matrix components are organized into a basal lamina, a thin sheet-like structure. Type IV collagen is the most important structural component of basement membranes and forms the basic fibrous two-dimensional network of all basal laminae. The structure of type IV collagen is characterized by three domains: the N-terminal domain, a large globular domain at the C-terminus, and the central helical segment with short interruptions (about 24 times) of the Gly-X-Y sequence with segments that cannot form a triple helix 5. These globular regions introduce flexibility into the molecule. These interactions, together with those between the C-terminal globular domains and the triple helices in adjacent type IV molecules, generate an irregular two-dimensional fibrous network 13.


The diversity among the collagen family members is mainly determined by the existence of several α-chains with different number of amino acids and how these structure associate together. Type I collagen is the most abundant in the human body: it forms more than 90% of bone organic mass and it is the major collagen of tendons, ligaments, cornea and many interstitial connective tissues. It is also the main component of human skin (80%) with type III collagen making up the remainder of skin collagen (15%) 5,10. The unique physical properties of collagen fibres confer structural integrity to the skin forming a dense network throughout the dermis. The main function of this network is to provide structural support to the epidermis. In addition, collagen and elastin together form the extracellular matrix, which gives the skin its structure, elasticity and firmness 11 (Figure 7). Collagen is recognised by the medical and scientific community for providing a structural support for most tissues in the body, and is particularly abundant in the connective tissue. Normal collagen formation is also required for the structure of many other tissues, including bones, cartilage, gums, tendons and blood vessels.


Figure 7. Diagram showing the structure of the skin.

The different layers of the are visible: epidermis, dermis and adipose tissue. Collagen fibres, elastin and fibroblasts are also represented. The collagen in the skin is mainly produced by fibroblasts. These are connective tissue cells in the dermis which are the main responsible for producing and organising the collagen matrix. Fibroblasts are sensitive to physical and chemical stimuli, which can induce both fibroblasts activation and proliferation. Chemical stimuli are based on a “key-lock” mechanism where small ligands bind receptors located on the fibroblast extracellular membrane inducing their activation 12. Physical stimuli are directly related to the interactions between collagen and fibroblasts (Figure 8). fibroblast-large

Figure 8. Fibroblasts activation that leads to collagen production.


  • The collagen family consists of 28 different proteins, which account for 25% - 35% of the total protein mass in mammals.
  • All 28 types of collagen contain a repeating Gly-Y-X sequence and fold into a characteristic triple-helical structure.
  • The various collagens types differ for the ability of their helical and non-helical regions to associate into fibrils, to form sheets, or to cross-link different collagen types.
  • Most collagen is fibrillar and composed of type I collagen molecules. A two dimensional network of type IV collagen is characteristic of basement membranes.
  • Fibrous type collagen molecules (type I, II and III) assemble into fibrils that are stabilized by covalent cross-links.
  • Procollagen chains are modified and assembled into a triple helix in the ER, inside the cell. The triple-helical molecules are then released through secretory vesicles into the extracellular space, where the collagen fibrils and fibres form.
  • Type I collagen is the main component of human skin (80%) with type III collagen making up the remainder of skin collagen (15%).
  • The collagen in the skin is mainly produced by fibroblasts. Fibroblasts are sensitive to physical and chemical stimuli, which can induce both fibroblasts activation and proliferation.


  1. Heino, J. in BioEssays : news and reviews in molecular, cellular and developmental biology Vol. 29   1001-1010 (2007).
  2. Matsuda, N. et al. Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis. Journal of nutritional science and vitaminology 52, 211-215 (2006).
  3. Myllyharju, J. & Kivirikko, K. I. Collagens and collagen-related diseases. Annals of medicine 33, 7-21 (2001).
  4. Ricard-Blum, S. The collagen family. Cold Spring Harbor perspectives in biology 3, a004978, doi:10.1101/cshperspect.a004978 (2011).
  5. Gelse, K., Poschl, E. & Aigner, T. Collagens--structure, function, and biosynthesis. Advanced drug delivery reviews 55, 1531-1546 (2003).
  6. Birk, D. E., Fitch, J. M., Babiarz, J. P. & Linsenmayer, T. F. Collagen type I and type V are present in the same fibril in the avian corneal stroma. The Journal of cell biology 106, 999-1008 (1988).
  7. Mayne, R. Cartilage collagens. What is their function, and are they involved in articular disease? Arthritis and rheumatism 32, 241-246 (1989).
  8. van der Rest, M. & Garrone, R. Collagen family of proteins. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5, 2814-2823 (1991).
  9. Bruckner, P. & Prockop, D. J. Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Analytical biochemistry 110, 360-368 (1981).
  10. Fleischmajer, R., MacDonald, E. D., Perlish, J. S., Burgeson, R. E. & Fisher, L. W. Dermal collagen fibrils are hybrids of type I and type III collagen molecules. Journal of structural biology 105, 162-169 (1990).
  11. Krieg, T. & Aumailley, M. The extracellular matrix of the dermis: flexible structures with dynamic functions. Experimental dermatology 20, 689-695, doi:10.1111/j.1600-0625.2011.01313.x (2011).
  12. Narayanan, A. S., Page, R. C. & Swanson, J. Collagen synthesis by human fibroblasts. Regulation by transforming growth factor-beta in the presence of other inflammatory mediators. The Biochemical journal 260, 463-469 (1989).
  13. Lodish H, Berk A, Zipursky SL, et al. Molecular Cell Biology. 4th edition. New York: W. H. Freeman; 2000. Section 22.3, Collagen: The Fibrous Proteins of the Matrix. Available from:

What is Hydrolysed Collagen?

Hydrolysed collagen consists of small peptides with low molecular weight. The quality of the final hydrolysed collagen is dependent on its average molecular size, which can vary based on the methodology used to extract it. Generally, collagen molecules are denatured and partially hydrolysed to form gelatin (100 kDa). Gelatin can then be decomposed into small peptides using specific proteins with cleavage activity (proteinase). The molecular weight distribution of collagen peptides usually span in the range 0.3 - 8 kDa.

Due to the low molecular weight, there are several advantages of using hydrolysed collagen with respect to native collagen: hydrolysed collagen can be dissolved in cold water; hydrolysed collagen is highly digestible; hydrolysed collagen is easily absorbed and distributed in the human body.


Pure GOLD COLLAGEN® contains a unique blend of the highest quality hydrolysed collagen extracted from fish, rich in specific amino acids: glycine, proline and hydroxyproline, which are easily absorbed by the body. Collagen peptides have two main functions: firstly they provide a natural source of amino acids and secondly they are biologically active and stimulate collagen production in the dermis. Replenishing these amino acids is essential to maintaining the amount of collagen, key to a healthy and youthful skin. Where does our hydrolysed collagen come from? Our hydrolysed collagen Peptan™ produced by Rousselot SAS of France contains a blend of the best quality hydrolysed collagen extracted from farmed Tilapia fish. All fish used by Rousselot only come from establishments registered by the European Union for the import of edible fish, fit for human consumption and guaranteed by health certificates signed by official veterinarians. Rousselot is a leading global manufacturer of ingredients for the food, pharmaceutical, food supplements and cosmetics markets. Watch the new Peptan™ Beauty video or for additional information please visit Rousselot's website

Hyaluronic Acid

Hyaluronic acid is found mainly in the skin where it plays a key role in skin hydration, due to its ability to bind water. Hyaluronic acid has a fast turnover rate and its level in the skin changes significantly during ageing.

It is important to restore normal hyaluronic acid levels in the skin to maintain skin hydration.

Hyaluronic acid (HA) is a high molecular weight polysaccharide, found mainly in the extracellular matrix of connective tissues [1]. The structure of hyaluronic acid is built from a linear combination of alternating units of Glucoronic acid and N-acetylglucosamine, with an average molecular weight ranging from 10 to 104 kDa [2, 3]. The molecular size is a key factor as this influences the physicochemical properties such as viscosity, elasticity and the ability to retain water. Hyaluronic acid has several physiological functions including lubrication, water homeostasis or cell proliferation. HA plays a key role in tissue hydration due to its ability to bind water molecules that can reach up to 1000 fold its molecular weight [1]. In addition, HA is found in a range of sizes and configurations and is able to interact with several other molecules, including proteins (e.g. collagen) or other glycosaminoglycans. HA is found mainly in soft connective tissues, in particular skin and joints. Experiments in vivo [4] have shown that approximately 50% of the total HA content is present in the skin. In the skin, HA is synthesised in the plasma membrane of fibroblasts, keratinocytes and other cells [1] by a membrane-bound protein: hyaluronic acid synthase. HA is found in the dermis but also in the epidermal intercellular spaces, especially in the middle spinous layer. Though HA is known to play a structural role in the connective tissue, its overall turnover rate appears to be surprisingly quick. Studies have shown that HA has a turnover rate from 0.5 to a few (2-3) days [1, 5]. The catabolism of HA takes place both by local degradation and drainage via the lymphatic system [5]. With age the density and the organisation of HA in the skin changes. Generally, aged skin, which is less plump than youthful skin, is characterized by a decreased levels of HA. However, different mechanisms have been observed in intrinsic and extrinsic ageing. Intrinsic aged skin is characterised by extracellular atrophy and the consequent loss of HA, which in turn affects the ability of the skin to retain water. Photo-aged skin instead is characterised by an increase in hyaluronic acid density, as observed by Bernestein et al [6]. However, though the density increases, HA is found to be abnormally deposited on elastoic material and this may interfere with its ability to bind water. Along with the different HA localisation, alterations in size, structure and conformation of HA may affect its water binding properties and as well its ability to interact with other components of the extracellular matrix. In conclusion, both intrinsic ageing and extrinsic ageing affect the normal HA function, which in turn determines a significant decrease in the hydration of the skin.  

Scientific Literature References

[1] Laurent, T.C. and J.R. Fraser. FASEB J, 1992. 6(7): p. 2397-404.

[2] Shimada, E. and G. Matsumura. J Biochem, 1975. 78(3): p. 513-7.

[3] Tammi, R., et al. . J Invest Dermatol, 1991. 97(1): p. 126-30.

[4] Reed, R.K., K. Lilja, and T.C. Laurent. Acta Physiol Scand, 1988. 134(3): p. 405-11.

[5] Fraser, J.R., T.C. Laurent, and U.B. Laurent. J Intern Med, 1997. 242(1): p. 27-33.

[6] Bernstein, E.F., et al. . Br J Dermatol, 1996. 135(2): p. 255-62.


How Ageing Effects the Skin

With age, the ability to replenish collagen decreases, hence the structure and elasticity of the skin degrades.

The human skin is composed of multiple layers. The outermost layer, the epidermis, acts as the skin's barrier to protect the body from the environment and external factors.

Deeper down is the dermis containing collagen, elastin fibres and fibroblasts. Collagen and elastin form the structure of the dermis making it tight and plump.

Fibroblasts are special cells that synthesize collagen and elastin. The subcutis is the deepest layer of the skin, composed primarily of fat.


Over 75% of young skin is made of collagen. With age, the ability to replenish collagen naturally decreases. The density of collagen and elastin in the dermis declines, hence the structure and elasticity of the skin degrades, causing it to become thinner and more rigid. The fall in collagen also results in the loss of hyaluronic acid. This reduces the moisture, suppleness and elasticity of the skin. The diminished elasticity of the skin reduces its ability to retain its shape and it does not conform as closely to the contours of the face. The skin appears looser and sags. Lines and furrows emerge to enable movement. Gravity then pulls on the skin, all leading to sagging eyelids, bags under the eyes, and jowls. The solution is Pure GOLD COLLAGEN®. The active ingredients reach the dermis from the inside, to re-activate collagen formation.

Skin ageing mechanism

Skin ageing is a complex biological process which affects several constituents of the skin and hence its appearance. There are two primary skin-ageing mechanisms, intrinsic and extrinsic [1-2]. Genetic variations are thought to be the main cause of intrinsic ageing, determining slow tissue degeneration, which result as time passes, "the biological clock". Extrinsic ageing instead is caused by environmental factors and in particular by sun exposure, also known as photo-ageing. Both intrinsic and extrinsic ageing act simultaneously and are associated with phenotypic changes in the skin (i.e. wrinkle formation). However, deep inside in the dermis, fibrillar collagens, elastin fibres and hyaluronic acid, which are the major components of the extracellular matrix, undergo different structural and functional changes. Collagen and elastin are long-life proteins and hence are pre-disposed to intrinsic molecular ageing. While the half-life* of many proteins is measured in hours, collagen and elastin have half-life measured in years [1]. As a consequence these fibres accumulate damage over time and this decreases their ability to function correctly. Intrinsically aged skin is generally characterised by dermal atrophy with reduced density of collagen fibres, elastin and hyaluronic acid. (Figure below, modified from reference [1]).


Structural changes in the dermis are more severe when the skin is both intrinsically old and photo-aged [1]. Extrinsically aged skin is characterised by degradation and alteration of collagen fibres and the accumulation of disorganised elastin proteins throughout the dermis, process also known as elastosis (Figure below, modified from reference [1]). Evidence indicates that the activation of matrix metalloproteinases play a major role in the pathogenesis of photoageing [3]. Metalloproteinases can be induced by UVA and UVB [4] and show proteolytic activity that results in the degradation of collagen and elastin fibres. As a result, the collagen density decreases each year with faster rate in photo-exposed skin [2]. Extrinsically aged skin is characterised by several clinical manifestation including leathery appearance, increased wrinkle formation, reduced recoil capacity, increased fragility of the skin and altered colour pigmentation.

* The half life is a prediction of the time it takes for half of the amount of a protein to be degraded.


Scientific Literature References

  1. E.C. Naylor, Maturitas, 2011, 69, 249-256
  2. Baumann, J Pathol, 2007; 211: 241–251
  3. El-Domyati M, Exp. Dermatology, 2002, 11: 398–405.
  4. M. Berneburg, Photodermatol Photoimmunol Photomed 2000; 16: 239–244

Clinical Trials

Pure GOLD COLLAGEN® has been clinically proven to be effective

A UK study carried out on 108 volunteers taking Pure GOLD COLLAGEN® daily showed: (a) 12% increase in skin hydration after three weeks; (b) 15% decrease in fine lines and 27% reduction in deep wrinkles, after 6 weeks); (c) 20% increase in skin elasticity after nine weeks. Reference AN2961: (Double blind, placebo controlled randomised clinical trial).

PGC Clinical Trial Results - Graphs


Pure GOLD COLLAGEN® acts from within

It boosts the level of collagen and hyaluronic acid in your skin.

  how it works

Pure GOLD COLLAGEN® contains a blend of hydrolysed collagen and active ingredients to act from within. The following provides an overview of the scientific evidence and the hypothesis related to how the hydrolysed collagen contained in Pure GOLD COLLAGEN®works. The hypotheses are based on extensive scientific literature.   A) When administered orally, hydrolysed collagen reaches the small intestine where it can be digested to form dipeptides and tripeptides or free amino acids.   B) These peptides are easily absorbed across the small intestine membrane [1] where they enter the blood stream [2, 3].   C) Through blood vessels collagen peptides are then distributed in the human body and in particular in the dermis of the skin [3, 4] where an in vivo experiment has proven that they can remain up to 14 days [4].     D) Once in the skin the collagen peptides can act with a double mechanism, i) Collagen peptides and free amino acids provide the building blocks for the formation of collagen and elastin fibres; ii) Collagen peptides stimulate the proliferation of fibroblasts [5,6] and the synthesis of collagen [5] and hyaluronic acid [6]. Based on the hypothesis drawn from the referred scientific literature the benefits of fibroblasts activation can be summarised as follows: I) Increased collagen synthesis. II) Increased hyaluronic acid synthesis.

Stimulating the fibroblasts is the key to increase the levels of collagen and hyaluronic acid in the dermis


Scientific Literature References

1. Aito-Inoue, M., et al., J Pept Sci, 2007. 13(7): p. 468-74.

2. Iwai, K., et al., J Agric Food Chem, 2005. 53(16): p. 6531-6.

3. Oesser, S., et al., J Nutr, 1999. 129(10): p. 1891-5.

4. Watanabe-Kamiyama, M., et al., J Agric Food Chem, 2010. 58(2): p. 835-41.

5. Chen, R.H., et al., Journal of Food and Drug Analysis, 2008. 16(1): p. 66-74.

6. Ohara, H., et al., J Dermatol, 2010. 37(4): p. 330-8.


Drinking vs Topical Use

The skin protects our body

It is extremely difficult to penetrate

The main function of the skin is to act as a barrier in order to protect the human body from the external environment. The outer layer of the skin is the epidermis, which is composed of multiple layers, with the stratum corneum being the outermost part. This layer is extremely difficult to penetrate and represent the first barrier to the external environment. As a result the chance of active ingredients to reach the dermis of the skin through topical application is very limited [1]. Many commercial products containing collagen (e.g. creams, serums), applied topically on the skin, claim the ability of acting in the dermis, where they would induce an increase in collagen levels. However, collagen is a large molecule (300 kDa) and cannot penetrate the epidermis [1], hence its effect is limited to the skin surface.

In order to reach the dermis, it is possible to act from the inside and the oral intake of hydrolysed collagen represents an effective solution to this problem.

how it works

It has been shown that collagen peptides, administered orally, can be digested, absorbed and then distributed to the inner layer of the skin, where they show high biological activity click here to read an interesting Daily Mail article titled 'Why collagen creams 'are money down the drain'  

Scientific Literature References

[1] Bos, J.D. and M.M. Meinardi, Exp Dermatol, 2000. 9(3): p. 165-9.