Bioactive Collagen Peptides in Veterinary and Biomedical Science—Part I: Molecular Identity, Gastrointestinal Bioavailability, and Receptor-Mediated Signaling, with Relevance to the Bile Acid Axis
The strongest current evidence supports specific collagen fragments for relieving joint disease in dogs and horses, and a newly recognised link between collagen fragments, gut bacteria, and bile that may explain effects on metabolism and the liver is described.
Abstract
Simple Summary Collagen is the main structural protein of skin, bone, tendon, and cartilage, and it was long viewed only as a building material. When collagen is broken into small fragments—during digestion or in collagen supplements—some fragments are absorbed into the blood and act as signals that influence the body well beyond the tissues they came from. This review, the first of two parts, examines what these small collagen fragments are, how efficiently animals absorb them, and which cell-surface sensors and internal pathways they switch on. The evidence comes from laboratory experiments, animal studies, and clinical trials, and we are careful throughout to separate firm clinical findings from early laboratory observations. The strongest current evidence supports specific collagen fragments for relieving joint disease in dogs and horses. We also describe a newly recognised link between collagen fragments, gut bacteria, and bile that may explain effects on metabolism and the liver. The main message for practice is that collagen supplements are biologically active compounds whose effects differ between species, so the dose and the expected benefit should be judged species by species rather than assumed from one animal to another.
Simple Summary Collagen supplements are usually thought of as joint or skin remedies, but the small collagen fragments released during digestion reach far more of the body than the joints alone. This review, the second of two parts, follows these fragments from the gut outward. In the intestine they help seal the gut lining, shift the balance of gut bacteria, and alter bile, the digestive fluid made by the liver. Through these routes they can influence appetite, blood sugar, fat tissue, the liver, and even the brain. We sort the evidence carefully, separating proven clinical results from promising early findings. The firmest veterinary evidence supports collagen fragments for joint disease in dogs and horses, and dietary taurine—a different nutrient that also works through bile—for a reversible form of heart-muscle disease in certain dog breeds. Newer laboratory work points to effects on fat-burning, memory, and blood clotting, but these still need confirmation in animals before any clinical claim. The practical message is that diet shapes a shared gut–bile signalling system, and that collagen and taurine act on it as separate dietary inputs, with real relevance for companion animals, horses, and livestock.
Krisztián Németh, Borbála Mózes, Tibor Bartha et al.· Veterinary Sciences· 0 citations
Across both in vitro and in vivo models, ultra-low molecular weight collagen (LMWCP), with more than 45% di- and tripeptides, exhibited faster early-phase absorption kinetics, thereby enhancing early-phase bioavailability.
Reyhan Nergiz-Unal, Stephan Dierckx, C. Roye et al.· PeerJ· 0 citations
Collagen peptides obtained from by-products have gained attention as functional ingredients due to their potential to interact with gut microbiota and related metabolic outcomes. This study characterized collagen peptides, extracted from chicken bones by enzymatic hydrolysis, and investigated how they interact with human gut microbiota using the dynamic SHIME® in vitro model. LC-MS/MS-based peptide profiling of the hydrolysate identified 286 peptides derived from 28 precursor proteins, predominantly with molecular weights <1500 Da and a high abundance of hydroxyproline. It was observed that the peptides treatment promoted a significant restructuring of the bacterial community in the ascending, transverse, and descending colon, stimulating the growth of genera such as Prevotella, Blautia, and Dorea while suppressing potentially pro-inflammatory microbial groups. The intervention also increased short-chain fatty acid production across sections during the 16-day treatment phase, particularly acetic (from 6.16 to 14.36 mM) and propionic acid (from 1.56 to 8.09 mM). Overall, these findings support the use of chicken bone-derived collagen peptides as a promising strategy to modulate gut microbiota ecology and metabolic outputs.
Rebeka Correia de Souza Cunha, I. Franciosa, Viviane Maria de Sousa Fontes et al.· Food & Function· 0 citations
Skin aging is a complex biological process characterized by a gradual decline in the structural integrity and physiological functions of the skin, leading to wrinkles and loss of elasticity. Collagen, the main structural protein in the extracellular matrix (ECM), plays a crucial role in maintaining skin strength and resilience. This article reviews the promising potential of bioactive collagen peptides derived from aquaculture by-products, specifically the skin of rainbow trout (Oncorhynchus mykiss), as effective anti-aging agents. Special focus is given to the mechanisms of action of these peptides at the level of human dermal fibroblasts, the primary cells responsible for collagen synthesis. The review discusses extraction and enzymatic hydrolysis methods, the physicochemical properties of the resulting peptides, their effect on type I collagen synthesis, inhibition of matrix metalloproteinases (MMPs), modulation of key cellular signaling pathways such as TGF-β and NF-κB, and their antioxidant activity. The collective evidence suggests that collagen peptides from rainbow trout skin are a valuable functional ingredient for cosmetic and nutraceutical applications and demonstrate high potential for the valorization of fishery by-products.
L. M. Rashid, V. S. Turitsin· Fisheries· 0 citations
This review assesses the critical role of the food matrix (FM) in regulating peptide bioavailability, addressing the new challenge of overcoming low oral absorption of diverse peptide classes and advocating for matrix-engineered delivery systems (such as microencapsulation and probiotic fermentation) to establish a holistic, matrix-aware approach to functional food design.
Chunhong Liu, Chao-Qing Wen, O. Olatunji et al.· The Journal of the Science o...· 0 citations
Collagen is the dominant structural protein of vertebrate connective tissues and a central biomaterial in skin, cornea, tendon, cartilage, bone, vessel, oral mucosa, and wound repair. Traditional collagen products have largely been extracted from bovine, porcine, fish, or other animal tissues. Although animal‐derived collagens have a long clinical history, they have limitations including batch variability, residual nonhuman epitopes, possible immunogenicity, pathogen‐related concerns, ethical constraints, and limited molecular engineering. Recombinant human collagen has emerged as a synthetic‐biology alternative designed to reproduce full‐length human collagen chains, selected human collagen domains, or engineered humanized collagen‐like sequences in controlled expression systems.
Kyu‐Ho Yi, J. Song, Hongseok Kim· Journal of Cosmetic Dermatol...· 0 citations