Fragmentation and disorganization of collagen fibrils are part of the skin ageing process. Healthy collagen fibrillogenesis is critical for healthy skin.  

Animal cells produce collagen that is rich in amino acids – glycine, proline, hydroxyproline and arginine. Collagen monomers are ~300nm long and ~1.36nm in diameter.  Millions of collagen monomers assemble to form cylindrical fibrils. 

It is interesting that collagen molecules nucleate and self-grow into fibrils in vitro, like salt crystallisation. However, it produces a randomly oriented gel without fibril length, number, or orientation restraints.  

Collagen fibril formation is very different in vivo. The three-dimensional arrangement, including the orientation, alignment, density and cross-linking determines its mechanical properties. Collagen fibrils can be thin, transparent, orthogonally arranged, as found in the cornea. They can also be thick, opaque, parallelly bundled, as found in tendons.  

To produce useful fibrils and tissues, cells secrete not just collagen but also various signalling proteins to guide the multi-step process. 

For example, Decorin binds to collagen fibrils, promoting their proper alignment and organization. Decorin-deficient mice have been shown to suffer from fragile skin. Cells secrete Fibulin to support copper ion transfer, which in turn catalyses the elastin-collagen cross-linking process. Our cells produce less Fibulin as we age, and after acute UVB irradiation. Lumican ensures that collagen fibrils grow at a controlled rate, preventing abnormalities in their size and structure.  Lumican-deficient mice have been shown to suffer from skin laxity and corneal opacity due to deregulated growth of collagen fibrils. 

Cells produce everything they need in the exact amounts and proportions for proper cellular functions. If we can produce a cell-identical mixture of the signalling proteins and turn them into smaller-sized multi-peptides to be absorbed by the skin, they can help cells in our epidermis for collagen fibrillogenesis.

Unfortunately, we cannot get these from plants. Plantae biological makeup is different from that of Animalia.  These signalling proteins appear in animal tissues, but in minute amounts, and chemical extraction cannot harness them.  Synthetic peptides are neither bioidentical nor sufficient for multiple cellular pathways.  Single protein molecules produced by recombinant technology are biologically similar. Yet, the molecule is only one of the hundreds of signalling proteins needed, resulting in limited benefits and overdosage risk.

With the advancement of biotechnology, it is possible to produce cell-identical multi-peptides. Zellulin^® BioPlatform is known as the pioneering patented technology that achieves exactly that. Cells are taken from a single fish and are used to produce an exponential number of additional cells inside a sterile bioreactor. Significantly, due to this cell cultivation technology, no additional fish or other animals are needed beyond this single initial fish. It is 100% traceable source-to-ingredient.

All signalling proteins are extracted from the cells and transformed into 500 Dalton or smaller biopeptide complexes. In vitro study showed that the cell-identical multi-peptides upregulate many skin-health-related genes. A 28-day placebo-controlled efficacy test showed statistically significant benefits of increased skin hydration, barrier, elasticity, firmness and dermal density. 

Zellulin^® ZelluGEN™ is a biopeptide complex that instructs skin cells to synthesise more extracellular matrix (ECM), the skin’s structural foundation. It is produced at an ISO22716-certified facility using a novel, sustainable process with full traceability. Zellulin^® ZelluGEN™ is proven to renew, protect, and maintain youthful skin. It is water-soluble and suitable for use as an advanced multifunctional active ingredient within anti-ageing formulations.

Get the Zellulin^® ZelluGEN™ Experience Kit now 

from https://portal.zellulin.tech/ while stock lasts, 

or contact sales@zellulin.tech.