A prerequisite for good mobility is to keep bones healthy. This holds true during ageing, where bones start to lose their strength and density, with higher risks of fractures that can affect quality of life. Older consumers are increasingly demanding proven, natural ingredients that can help enforce bone health. Today, the medicines commonly used to treat bone related conditions have been shown to have poor therapy compliance and the benefits do not always continue after the end of treatment. The growing ageing population and associated costs to the individuals and society call for an urgent solution with early prevention to avoid or delay limitations of skeletal functions being the preferred option compared to cure.
The benefits of protein to meet the rising challenge of bone health are well documented—protein fortification at the right levels and modality can play a crucial role in bone development, with a direct impact on bone mineral density and skeletal microarchitecture. More specifically, a recently-published scientific review has highlighted the growing bank of evidence on the benefits of collagen fortification in managing bone health—analysing products such as collagen peptides as a bioactive protein.
In the bone health space, an increasing focus is being put on early prevention to avoid or delay any limitations of the skeletal functions, which may lead to mobility problems. Alternative prevention strategies are therefore being explored with nutritional supplementation with collagen peptides as a widely-accepted, safe means of maintaining good bone health. The goal of a nutritional strategy to prevent bone loss is providing sufficient constitutive elements, such as the amino acids included in collagen. Collagen represents about 80 percent of the total protein content of bones and it plays a crucial role in their capacity to resist mechanical forces and fractures, making it a primary nutrient in bone health products.
Healthy bones for longer
Age-related bone fragility is often attributable to alterations of the collagen network. In this context, evidence from animal models has found collagen peptide supplementation can help replenish the collagen structure in bones. For example, one in vivo study carried out with one brand of collagen peptides recorded that supplementation significantly contributed to the increase of bone mineral density and bone strength. A second in vivo study showed that the administration of collagen peptides for three to six months prevented bone loss in ovariectomised mice, the bone-health equivalent of post-menopausal women. Altogether, these and additional studies provide a solid body of evidence of the potential for collagen peptides to maintain a balanced bone turnover.
To date, the relationship between collagen supplementation and bone metabolism have been an important section of bone health research, which highlights the positive links between collagen and osteoblastic differentiation, an important step in bone formation where collagen peptides may serve as an effective supplement to prevent bone loss and support the strengthening of bone matrix.
Bioavailability and additional benefits
Collagen peptides are hydrolysed and highly bioactive form of collagen, digested in the gut and entering the circulation through the intestinal barrier. It has been widely shown collagen peptides, as opposed to the intact form, improve the absorption of amino acid availability and delivery to target tissues.  The effects of collagen peptides also indicate improvements in calcium absorption—an essential mechanism in preserving bone capital. A combination of studies suggests dietary protein works synergistically with calcium to improve calcium retention and bone metabolism. As such, collagen peptides could also offer additional value to the supplementation of vitamin D for bone health, addressing the growing demand for preventative, multi-ingredient nutritional supplementation.
The in-depth review, published in 2017, demonstrates collagen peptides stimulate bone forming cells, improves calcium absorption and has anti-inflammatory and antioxidant properties, which could all prove key in the improvement of bone health in the future.
Dr Elke De Clerck holds a PhD in Biotechnology from Gent University. With over 10 years’ experience in the food and pharma industries, Elke has held positions in product management, new product development and business development. She has worked for Rousselot for the last seven years in a number of technical and business development roles, which have had a key focus on nutrition. Currently, Elke is responsible for the global market development of Peptan, Rousselot’s brand of collagen peptides.
 Coxam, V., et al., 2008. Nutrition et metabolisme osseux. In: Aliments Fonctionnels. pp. 729–798. Lavoisier, Ed.
 Daneault, A. et al., 2017. Biological effect of hydrolyzed collagen on bone metabolism. Critical Reviews in Food Science and Nutrition, 57(9):1922-1937
 Tzaphlidou, M., 2005, The role of collagen in bone structure: An image processing approach. Micron. 36(7):593–601
 Guillerminet, F. et al., 2010, Hydrolyzed collagen improves bone metabolism and biomechanical parameters in ovariectomized mice: An in vitro and in vivo study. Bone, 46: 827-834
3. Guillerminet, F. et al., 2012, Hydrolyzed collagen improves bone status and prevents bone loss in ovariectomized C3H/HeN mice. Osteoporosis International, 23(7):1909-1919
Guillerminet, F., et al., 2012, Hydrolyzed collagen improves bone status and prevents bone loss in ovariectomized C3H/HeN mice. Osteoporosis International 23 (7): 1909-1919
 Ichikawa, S. et al., 2010, Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatine hydrolysate. International Journal of Food Sciences and Nutrition, 61 (1):52-60
 Shigemura, Y. et al., 2014, Dose-dependent changes in the levels of free and peptide forms of hydroxyproline in human plasma after collagen hydrolysate ingestion, Food Chemistry, 159:328-332
 Watanabe-Kamiyama, M. et al., 2010. Absorption and effectiveness of orally administered low molecular weight collagen hydrolysate in rats. Journal of Agricultural and Food Chemistry, 58:835-841