DivaLab Collagen Tripeptides 500 Da bovine medical food 30 servings 153 g

Preparate for dietary management

DivaLab® Collagen Tripeptides 500 Da is an advanced technologically developed medical purpose food in powder form, intended for dietary management in adults with specific nutritional needs arising from clinical conditions, particularly in the post-operative period, including after aesthetic medicine procedures, orthopaedic surgeries, bariatric operations, and stomach resections, as well as during convalescence when there is an increased demand for protein due to intensified regenerative processes, tissue healing, collagen synthesis, and the need to maintain the proper structure of the dermis.

The preparation provides a concentrated source of protein in the form of collagen tripeptides with an ultra-low molecular weight of approximately 500 Da, rich in glycine, proline, and hydroxyproline, in the form of di- and tripeptide fractions with documented oral bioavailability.

The formula has been enriched with vitamin C, which contributes to normal collagen production to support the proper functioning of bones, cartilage, and skin.

This product is used in professional practice within aesthetic medicine, cosmetology, and physiotherapy focused on tissue work, as a component supporting skin and tissue quality parameters.

The collagen tripeptides used in the product hold certifications including FSSC 22000, ISO 9001:2015, ISO 22000:2018, TS OIC/SMIIC 1:2019, and Halal Food Standard.

Medical Purpose Food (MPF, FSMP) - application in dietary management
In the mentioned clinical situations, maintaining a stable daily protein intake that complies with recommendations is often challenging, even with a properly planned diet. In practice, limited volume tolerance of meals, rapid satiety, selective tolerance of certain protein sources, and functional limitations in preparing and consuming complete meals mean that simply increasing the number or volume of high-protein meals is often not a feasible option.

This is especially important during periods of increased protein demand, such as in aesthetic medicine and professional cosmetology procedures, where controlled disruption of tissue structures triggers physiological skin remodelling processes, as well as during convalescence after orthopaedic procedures, immobilisation, and intensive rehabilitation.

In these situations, the need for building blocks, including amino acids used in collagen synthesis, is increased, while the ability to provide adequate protein intake through a standard diet remains limited. This affects both skin tissues and musculoskeletal structures, where remodelling processes require sufficient nutrient supply to support proper tissue structure.

Additionally, some patients, especially after bariatric surgeries and procedures involving the upper gastrointestinal tract, may experience altered digestion and absorption physiology, which can impair protein utilisation. Disruptions in synchronisation between food intake and digestive enzyme secretion, as well as accelerated intestinal transit, can reduce the efficiency of amino acid digestion and absorption.

This may decrease tolerance to standard high-protein product portions, often accompanied by gastrointestinal discomfort that further complicates dietary adherence. In such cases, using protein in the form of short peptides, which do not require complete digestion into free amino acids before absorption, offers a form better suited to the altered gastrointestinal physiology, especially under conditions of limited volume tolerance.

The collagen tripeptides with a molecular weight of 300-500 Da provide a specific pool of collagen amino acids (glycine, proline, and hydroxyproline) as a building material for the synthesis of new collagen fibres and short signalling peptides involved in the physiological remodelling of the extracellular matrix in collagen-rich tissues, including the dermis.

The presence of short collagen peptides also aligns with the body's natural mechanisms for extracellular matrix remodelling in both the skin and musculoskeletal structures. In the dermis, collagen forms the primary scaffold of the extracellular matrix, responsible for its density, elasticity, and water-binding capacity, which are crucial for qualitative skin remodelling rather than just short-term surface effects.

The addition of vitamin C completes the formulation as an essential cofactor in the hydroxylation of proline and lysine in procollagen chains. Vitamin C contributes to normal collagen production and supports cellular protection against oxidative stress, which is particularly important during periods of increased tissue turnover.