MAINTAINING COLLAGEN STRUCTURE IS KEY TO BEAUTY
After the age of 30, fine lines, wrinkles and loss of elasticity are common symptoms associated with skin aging. Build-up of environmental exposure and a natural decrease in cell renewal contribute to other signs associated with aging such as dry skin and a loss of natural shine (1).

WHAT IS COLLAGEN?

Collagen is a protein formed by a triple helix structure of amino acids,
which makes up the support fibres of the body.



Collagen is the most abundant protein in the human body, representing 25% of its total proteins. It is also the largest constituent of connective tissue, i.e., skin, cartilage, tendons and bones. Collagen is synthesised by fibroblasts (skin cells), chondrocytes (cartilage cells) and osteoblasts (bone cells). There are 23 types of collagen; types 1 and 3 are those present in the skin (2,3).

Concerning its shape, collagen is an extremely elastic protein. As such, it can fulfil its function of maintaining the strength and elasticity of the skin, bones, muscles, tendons and ligaments, thereby preventing fractures, sprains and breaks related to these structures. The constant repair of collagen structures favours the maintenance of the skin’s shine and softness, preventing the formation of furrows that lead to wrinkles (2,4).

It is easy to observe a deficiency in collagen and connective tissue. The changes that occur due to advancing age are directly related to changes in the quality and quantity of this protein. When the connective tissue that serves as a structural basis becomes stiff and less elastic, atrophy, wrinkles and weariness begin to appear on the surface of the skin (1).

YOUTH vs. OXIDATIVE STRESS

What are some of the so-called "enemies" of beauty?

Excessive sun, cigarettes and toxins can all affect the elasticity of skin. Another factor that has also been directly linked to skin aging is glucose. Glucose is fundamental to a cell’s life, as it serves as its fuel. However, by observing the speed at which diabetic individuals age, it became evident that chronic exposure to this simple carbohydrate in the body stimulates a process called glycation (5).

Glycation is a chemical process that occurs within the body, a reaction between a protein (collagen) and a carbohydrate (glucose) when they meet. This reaction causes the collagen to be destroyed and in the process lose its sustainability function (6-8). Evidence also shows that glycation reactions are accelerated by oxidative stress in skin cells (9), which acts as the main factor in the events that trigger skin aging in the cell (4).

Average Value Comparison Of Amino Acids From Three Protein Sources (3)



% OF AMINO ACIDS

Collagen Peptides

Whey Protein Concentrate

Soy Been
Isolate Protein

Glycine

20

1.5

4

Hydroxyproline

12

0

0

Proline

13

4

5

WHAT IS OXIDATIVE STRESS?

"The oxygen we breathe naturally generates oxidising compounds within our cells. [This] is a necessary process for the generation of energy and for the cells to remain alive. To combat these compounds, the body has developed an antioxidant system, which [can be described as] a "dirty and wash" cycle. It is enzymes, proteins, vitamins, and minerals that recover the cell and maintain our vitality. Over time, the body is no longer the same and cannot easily recover, needing external help to repair its tissues" (10).

The infamous "free radicals" are able to break up (collagen) proteins, change the skin’s renewal cycle, damage DNA and promote the release of pro-inflammatory cytokines – the primary triggers in the production of inflammatory changes of the skin (4,11-14).

The main reason behind the benefits of collagen supplementation is the presence of amino acids that are not commonly found in food or in conventional protein supplements, such as whey protein. These are: glycine, proline and hydroxyproline – the primary constituents of collagen. A common characteristic of all collagen is its peptide sequence, which can be expressed as (Gly-X-Y), where Gly is glycine and X-Y are often represented by proline (Pro) and hydroxyproline (Hyp), respectively. This sequence is necessary for collagen to establish fibrils, which are in turn organised to form fibres, providing structural integrity to the extracellular matrix of connective tissue.

COLLAGEN AND HORMONAL FACTORS

In addition to producing a smaller quantity of collagen than men, women may also suffer from hormonal issues. The deficiency of sex hormones (oestrogen, testosterone, DHEA) and of the growth hormone, which occurs in women at around age 45-50, reduces the production of fibroblasts (cells that produce collagen). Without tissue elasticity, blood does not travel at the same speed or at the same flow, reducing blood supply to the cells, the skin and the sebaceous glands. These hormones in particular have a profound effect on the skin (15-23).

Aging, glycation, oxidative stress and hormonal decline: what can I do to combat these?

Together, these processes are responsible for deteriorating the skin's collagen, draining reserves of vitamin A and C and all other antioxidant resources we produce and ingest in order to maintain beautiful skin. Removing the primary trigger factors and providing the correct nutrients for normal skin repair and its cells are evidenced by numerous scientific studies to combat the deterioration of collagen. Thus, the field of nutrition takes advantage of the benefits of hydrolysed collagen, or collagen peptides, which are small amino acid groups that are obtained from type 1 collagen through a production process using the latest technology and the strict control of chemical and enzymatic hydrolysis. In this way, collagen absorption and its delivery to the skin can be facilitated (3). These specific amino acids will function in the desired area of the body, providing several benefits.

How do you get collagen from food?

We can get amino acids and specific nutrients for the formation of collagen by consuming protein sources such as meat (red, poultry and fish), from proteins in general (gelatine and protein supplements), in citrus fruits and other sources of vitamin C (orange, strawberry, kiwi, lemon, cherry and pineapple), and from primary sources of vitamin E (extra-virgin olive oil and fish).

Is gelatine a good source of collagen?

Although gelatine is a source of collagen, its hydrolysis is different from that of bioactive peptides, resulting in a protein with a large molecular weight that is difficult to digest. If its consumption is not accompanied by the intake of essential nutrients for its re-synthesis in the body (as is the case in, e.g., vitamin C and E), its function within the body may be impaired. In addition, essential nutrients for skin structure and cartilage, such as silicon, are equally important and should be part of a daily diet, and these are not found in gelatine.

What is the difference between collagen hydrolysate and collagen peptides?

Hydrolysed collagen is produced by the chemical hydrolysis (breaking of a large molecule into smaller pieces through enzymatic action) of animal collagen (bovine, swine or from birds). This process of hydrolysation is not controlled and as such, presents different sizes of molecules with different degrees of absorbency, a process that has to date not been well documented.

Collagen peptides are known as high quality collagen hydrolysates, wherein the degree of hydrolysis and the size of the resulting peptides are known and studied. The raw material for obtaining collagen peptides, as well as gelatine, is collagen protein. Collagen peptides, however, are relatively small molecules, with a molecular weight of less than 10 000 daltons. Peptides are composed of at least two and a maximum of 100 amino acids. These are characterised by excellent solubility in cold water and different from gelatine, do not form gels, even in highly concentrated solutions. One example is Peptan®, a product of collagen peptides with high absorption properties, due to its relatively small molecular size (2 000 to 5 000 daltons).

HOW DO COLLAGEN PEPTIDES IMPROVE SKIN?

These collagen peptides are extremely effective at improving the appearance of the skin. Studies have evaluated the intake of 10g of collagen peptides per day and compared it to a control group that did not consume this protein. Significant results were obtained in the group that consumed collagen peptides, including: skin hydration rose from 28% to 91% after eight weeks of use; a 41% to 77% reduction of microridges after six weeks of consumption; a 17% reduction of the total wrinkled surface in 68% of the group after 12 weeks. The control group showed a 30% increase of deep wrinkles after 12 weeks of study. Therefore, the intake of collagen peptides is closely related to indicators of beautiful skin such as increased hydration and improved softness, thanks to a reduction of microridges and the prevention of deep wrinkles. These benefits are related to the stimulation of the endogenous production of collagen caused by the consumption of peptides, due to their unique composition of peptides and amino acids (3). They can act as a source of protein and also contain specific amino acids that are essential to the skin.

SUPPLEMENTATION WITH COLLAGEN PEPTIDES, VITAMINS AND MINERALS

Food is not always sufficient for providing the optimal amount of nutrients that our body needs after the age of 30, or when signs of aging such as those mentioned above begin to appear.

Proksch and colleagues conducted a study to assess whether collagen peptides are effective in reducing signs related to skin aging. The study evaluated 69 women aged between 35 and 55 years. The researchers found that the supplementation of 2.5 g or 5.0 g of collagen peptides once a day for eight weeks significantly improved the elasticity of the skin of female participants (24). However, the investigators emphasise that the formation of collagen in the skin, sourced from both food and supplements, is associated with the intake of other nutrients such as vitamin C and silicon (25-27).

References:
1. Varani J,Dame MK, Rittie L, Fligiel EG, Kang S, Fisher GJ, Voorhees JJ. Decreased Collagen Production in Chronologically Aged Skin. American Journal of Pathology, Vol. 168, No. 6, June 2006.
2. 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: http://www. ncbi.nlm.nih.gov/books/NBK21582/
3. Rousselout. Benefícios da ingestão de Peptídeos de Colágeno (Benefits of Collagen Peptide intake) PeptanTM.
4. Masaki, H., et al. Role of antioxidants in the skin: anti-aging effects. J Dermatol Sci (2010): 85-90.
5. van Boekel MA. The role of glycation in aging and diabetes mellitus. Mol Biol Rep. 1991 May;15(2):57-64.
6. Pageon H et al. Collagen glycation triggers the formation of aged skin in vitro. Eur J Dermatol. 2007 Jan-Feb;17(1):12-20. Epub 2007 Feb 27.
7. Pageon H et al. Reconstructed skin modified by glycation of the dermal equivalent as a model for skin aging and its potential use to evaluate anti-glycation molecules. Exp Gerontol. 2008 Jun;43(6):584-8. Epub 2008 Apr 7.
8. Pageon, H. “Reaction of glycation and human skin: the effects on the skin and its components reconstructed skin as a model.” Pathol Biol . (2010): 226-31.
9. Kikuchi S et al. Glycation- a sweet tempter for neuronal death. Brain Res Brain Res Rev. 2003 Mar;41(2-3):306-23.
10. Barbosa KB, et al. Stresse oxidativo: conceito, implicações e fatores modulatórios. (Oxidative stress: concept, implications and modulatory factors). Rev. Nutr. vol.23 no.4 Campinas July/Aug. 2010.
11. Burke, KE., et al. “Synergistic damage by UVA radiation and pollutants.” Toxicol Ind Health (2009):219-24.
12. Fisher, et al. “Collagen fragmentation promotes oxidative stress and elevates matrix metallopreinase-1 in fibroblasts in aged human skin.” Amer J Pathol (2009) 101-114.
13. Pascucci, et al. “Role of nucleide excision repair proteins in oxidative DNA damage repair: an updating.” Biochem (2011): 4-15.
14. Rock, K., et al. “Collagen fragments inhibit hyaluronan synthesis in skin fibroblasts in response to ultraviolet B (UVB): new insights into mechanisms of matrix remodeling.” J Biol Chem (2011): 18268-76.
15. Chahal, HS., et al. “The endocrine system and ageing.” J Pathol (2007):173-80.
16. Makrantonaki, E., et al. “Skin and brain age together: The role of hormones in the ageing process.” Exp Gerontol (2010): 801-13.
17. Makrantonaki, E., et al. “Androgens and ageing of the skin.” Curr Opin Endocrinol Diabetes Obes (2009): 240-5.
18. Ramos-e-Silva, M., et al. “Elderly skin and its rejuvenation: products and procedures.” J Cosmet Dermatol. (2007): 40-50.
19. Verdier-Sévrain S. “Effect of estrogens on skin aging and the potential role of selective estrogen receptor modulators.” Climacteric. (2007): 289-97.
20. Hall G, et al. “Skin and hormone therapy.” Clin Obstet Gynecol (2004): 437-449.
21. Phillips, T J., et al. “Hormonal effects on skin aging.” (2001): 661-672.
22. Kanda, N., et al. “Regulatory roles in sex hormones in cutaneous biology and immunology.” J Dermatol Sci (2005): 107.
23. Raine-Fenning, NJ., et al. “Skin Aging and menopause; implications for treatment.” (2003); 371-8.
24. Proksch E, Segger D, Degwert J, Schunck M, Zague V, Oesser S. Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo- controlled study. Skin Pharmacol Physiol. Epub 2013 Aug 14.
25. Orbe J, Rodríguez JA, Arias R, Belzunce M, Nes- pereira B, Pérez-Ilzarbe M, Roncal C, Páramo JA. Antioxidant vitamins increase the collagen content and reduce MMP-1 in a porcine model of atherosclerosis: implications for plaque stabilization. Atherosclerosis. 2003 Mar;167(1):45-53.
26. Boyera N, Galey I, Bernard BA. Effect of vitamin C and its derivatives on collagen synthesis and cross-linking by normal human fibroblasts. Int J Cosmet Sci. 1998 Jun;20(3):151-8.
27. Peterkofsky B. Ascorbate requirement for hydroxylation and secretion of procollagen: relationship to inhibition of collagen synthesis in scurvy. Am J Clin Nutr. 1991 Dec;54(6 Suppl):1135S-1140S.
28. Zague V, de Freitas V, da Costa Rosa M, de Castro GÁ, Jaeger RG, Machado-Santelli GM. Collagen hydrolysate intake increases skin collagen expression and suppresses matrix metallopreinase 2 activity. J Med Food. 2011;14(6):618-24.
29. Faipoux, R. 2007. Characterization of the satieting effect of proteins and central mechanism implicated - Particular case of the yeast peptides and proteins. INA - Paris- -Grignon.
30. Zague V. A new view concerning the effects of collagen hydrolysate intake on skin properties. Arch Dermatol Res. 2008;300(9):479-83.