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Osteoarthritis (OA) is becoming one of the most common joint conditions due to increased life expectancy, representing a significant socioeconomic and public health problem. OA is characterized by inflammation and progressive destruction of articular cartilage, affecting any joint, although it is most common in the knee, hip, spine, and interphalangeal joints, causing pain, functional limitations, and a reduced quality of life.

Gelatin is probably the most common form of gelatin on the market, but no biological function for joint health has been described. However, it has excellent physical and mechanical properties, such as low solubility and ease of handling, mainly because it is composed of a mixture of peptides with different molecular weights. Therefore, gelatin is widely used in the manufacture of various food systems, such as capsules and films.

Hydrolyzed collagens are composed of amino acids and peptides of varying lengths (including dipeptides and tripeptides) that resist intracellular hydrolysis, preventing their degradation by peptidases and systemic hydrolytic enzymes. Thus, hydrolyzed collagen peptides have high bioavailability, allowing them to reach the bloodstream, accumulate in cartilage tissue, and induce the synthesis of extracellular matrix (ECM) in cartilage, stimulating chondrocytes.

The differences in the mechanisms of action described for native and hydrolyzed collagens could theoretically justify a possible combination of both types of collagen to explore their complementary effects.

Type II collagen (the main protein of articular cartilage) has been shown to be a potential source of autoantigens in osteoarthritis (OA). Consequently, oral tolerance to type II collagen could theoretically have a positive impact on controlling inflammation in OA. In fact, the efficacy of oral administration of low doses of native type II collagen has been demonstrated in animal models of osteoarthritis (OA), such as the monoiodoactetate-induced (MIA) rat model of OA. In this model, oral administration of native chicken type II collagen (1 to 10 mg/kg) reduced joint pain and decreased plasma concentrations of inflammatory cytokines (TNFα, IL-1β) and C2C levels.

Hydrolyzed collagen has been shown to contain biologically active peptides that can reach joint tissues and exert chondroprotective effects. Preclinical and clinical studies have demonstrated the safety and efficacy of ingredients containing native type II collagen or hydrolyzed collagen. However, available research suggests a clear link between the chemical composition/structure of collagen ingredients and their mechanism of action/efficacy.

https://www.mdpi.com/2072-6643/15/6/1332 (2023).--

https://pubmed.ncbi.nlm.nih.gov/39212129/ (2025)

https://keele-repository.worktribe.com/output/1230539 (2025)

https://www.tandfonline.com/doi/full/10.1080/09581596.2025.2588891 (2026)

https://assets.cureus.com/uploads/review_article/pdf/485824/20260621-42594-h9o4oy.pdf (2026)

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