Collagen-Derived Peptide Research


Research data suggests the impact of novel functional supplements comprising collagen peptides, vitamins, minerals, and antioxidants. Here, using a novel, physiologically relevant cell culture model crowded with macromolecular dextran sulfate, researchers analyzed the potential impact of collagen peptides and other constituents present in liquid collagen-based nutraceuticals on the normal function of primary dermal fibroblasts.  

The findings of this experiment implied that collagen peptides may boost fibroblast elastin production, whereas MMP-1 and MMP-3 release and elastin breakdown appeared dramatically decreased. Studies suggest that the antioxidant components of the products seemed to amplify the impact of the collagen peptides on these responses and fibroblast growth. These findings provide a cell-based explanation for why collagen-based nutraceutical supplements may positively impact the skin, and they point to the possibility that such substances may lead to the increased production of stable dermal fibroblast-derived extracellular matrices. 


In the extracellular matrix (ECM), interactions between cells, cytokines, and growth factors control the skin’s biophysical properties. Collagen type I, which forms fibrils, is believed to account for 90% of the skin’s collagen and is considered crucial to the skin’s structural organization, integrity, and strength. The dermis supports the epidermis with its intricate network of collagen fibrils, which, together with elastin and microfibrils, contribute to the skin’s elasticity and resilience. Hyaluronic acid, other polysaccharides, and proteoglycans are essential for skin moisture. 

Dermal fibroblasts release TGF, a versatile growth factor that regulates the production, deposition, and turnover of skin extracellular matrix proteins, including Collagen I, elastin, and proteoglycans. When fibroblasts are subjected to enough mechanical strain, they produce large amounts of collagen and other extracellular matrix components. When this tension decreases, as with age, matrix protein synthesis decreases, and matrix degradation enzymes increase. MMP-1, MMP-8, and MMP-134 are collagenolytic matrix metalloproteinases that may degrade the mature interstitial collagen fibrils despite their resistance to most proteolytic enzymes. The metalloelastase MMP-12 is found in macrophages, whereas the fibroblast-expressed MMP-3 is weakly elastolytic. 

Histopathological and immunohistochemical changes are related to intrinsic (chronological) and extrinsic (environmental and lifestyle variables such as UV radiation) skin aging. Cell senescence and changes in collagen, elastin, and glycosaminoglycans, including hyaluronic acid, are hallmarks of intrinsic aging. Loss of reticular collagen and increased disorganized elastic fibers and glycosaminoglycans characterize extrinsic aging. The expression of matrix metalloproteinases and collagenases is upregulated, and the extracellular matrix is altered in photo-aged skin (UV-irradiated skin). UV has been suggested to directly affect the integrity of elastic microfibril-related proteins and the elastin network, and increased production and activity of MMPs, including MMP-1, MMP-3, and MMP-9, has been linked to photo-aging. 

Peptides and Aging 

Decreased antioxidant defenses, resulting in higher levels of intracellular reactive oxygen species (ROS), are considered a primary cause of age-related skin damage. Aerobic metabolism generates these, promoting signal transduction, elevated MMP expression, and reduced collagen I synthesis. Protein damage and increased MMP expression and activity have been linked to ROS production in intrinsically and extrinsically aged skin. In addition, ECM proteins may act as skin photo-sensitizers and so contribute to skin photo-aging.  

Glycation, the development, and accumulation of AGEs (advanced glycation end-products) are hallmarks of age-related diseases and occur due to an age-related imbalance between the synthesis and degradation of ECM proteins. In addition, the capacity to regenerate collagen diminishes at around 1% yearly. Therefore, antioxidants may help prevent age-related damage caused by reactive oxygen species. Similarly, it has been suggested that reducing oxidative stress in a mouse model of advanced age may provide the animals antioxidants.  

The presentation of collagen peptides derived from hydrolysis of native porcine and piscine collagen has been hypothesized to improve the density and integrity of the collagen network, hydration, and elastic properties of normal skin, as suggested by data from placebo-controlled experimental studies. In addition, scientists purport that the look of aged skin may be enhanced by additional substances containing a combination of piscine collagen peptides and other active components such as hyaluronic acid, antioxidants, vitamins, and minerals. Cellular processes supporting these findings, however, have yet to be identified. 

Peptides and Aging: Research 

The purpose of one in vitro study was to examine the possible impact of collagen bioactive peptides, both alone and in combination with other bioactive compounds found in two different collagen-based nutraceutical compounds, on normal dermal fibroblast synthesis of collagen I and elastin, the release of transforming growth factor- (TGF-), plasminogen activator inhibitor-1 (PAI-1), matrix metalloproteinases (MMP), MMP-1 and MMP-3. 

Researchers hypothesized that these compounds’ antioxidant activity may interact with the collagen peptides’ potential impact to improve matrix proteins’ stability by reducing the release of matrix metalloproteinases (MMPs)-1 and MMP-3 in dermal fibroblast culture. 

Researchers interested in finding collagen peptides for sale for their scientific studies are encouraged to navigate the Core Peptides website. 

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