What is CTP | My Site 5

Synthetic Peptides (Collagen Tripeptides) – Mechanism of Action at Cartilage

1. Structural Characteristics

All collagens consist of three polypeptide chains (α-chains) arranged in a triple helix.
Each chain is composed of repeating Gly–X–Y sequences:
- X is often proline or lysine,
- Y is often hydroxyproline or hydroxylysine.
Glycine at every third position enables the tight packing of α-chains.
Providing a pool of these amino acids enhances type II collagen synthesis by chondrocytes and supports collagen reorganization, thereby slowing cartilage destruction in osteoarthritis (OA).

Animal-derived collagen contains potential antigenic sites:
- Red circle: Telopeptide region
- Blue circle: Glycosylation site
Collagen Tripeptide (CTP):
- Highly purified,
- Non-antigenic,
- Composed exclusively of Gly–X–Y sequences.

Small collagen-derived peptides have been reported to possess growth factor-like activities.
CTP stimulates chondrocytes to increase type II collagen gene expression (in vitro evidence).
When administered intra-articularly:
- Suppresses cartilage matrix loss,
- Prevents proteoglycan degradation,
- Promotes new extracellular matrix (ECM) synthesis.

Combination of CTP + hyaluronic acid + amino acids leads to:
- Enhanced fibroblast proliferation,
- Increased collagen biosynthesis,
- Stimulation of growth factor production.
Result: Accelerated cartilage and connective tissue regeneration.

Collagen Tripeptides (CTP) are highly purified, non-antigenic peptides with direct biological activity.
By stimulating type II collagen synthesis, promoting ECM production, and protecting cartilage from degradation, CTP offers a dual protective and regenerative mechanism in osteoarthritis and other cartilage-related conditions.

Collagen Tripeptides and Their Physiological Activities at soft tissue

Prolyl-4-hydroxyproline (Pro-Hyp) and Ala–Hyp Gly stimulate fibroblast proliferation, while Pro-Hyp, Ala–Hyp–Gly, and Leu–Hyp–Gly enhance collagen secretion in preosteoblasts and tenocytes
Hyp–Gly promotes myogenic differentiation and myotube hypertrophy
Leu–Hyp–Gly demonstrates strong angiotensin-converting enzyme (ACE) inhibitory activity
Pro-Hyp is shown to be generated by the degradation of endogenous collagen in granulation tissue to activate cells involved in tissue reconstruction/remodeling
Resident tendon cells (“tenocytes”) originate from multipotent mesenchymal cells and actively produce unique and tendon-specific ECM .
Studies to date have identified a requirement for Hyp-containing peptides in tenogenic differentiation and tenocyte maturation.
The glycine stimulated the synthesis of hydroxyproline, glycosaminoglycans, non-collagenous proteins and appeared to maintain or improve the organization of collagen molecules.
The biomechanical results indicated that the tendon was more resistant to mechanical loading upon treatment with a glycine.
Glycine also induced a rapid remodeling of tissue when compared with the groups without treatment. The data from this study suggest that glycine may be a useful therapeutic adjunct for individuals with inflammatory injuries of tendons, such as Achilles tendon injuries, and other types of connective tissue injuries and inflammatory events

Animal-derived collagen contains antigenic regions:
Telopeptides
Glycosylation sites
Collagen Tripeptides (CTP) are highly purified and non-antigenic, containing only Gly–X–Y tripeptide sequences.