Replicine has evolved from decades of scientific research. Built on a knowledge base of 40 years at the forefront of keratin and wool science, 20 years of fundamental and applied keratin science has created a remarkable technology platform and manufacturing base to delivery Replicine™ Functional Keratin technology solutions across a range of personal care, health care, nutritional and industrial applications.
Replicine is different from other keratin related technologies in three important ways, each of which affects the physical and biological performance of products incorporating Replicine keratin technology.
Respect nature’s complexity
Nature has evolved a family of keratin proteins with different family members chosen for different roles. In hair, the fibrous keratin intermediate filaments are responsible for tensile strength, whereas the globular keratin matrix proteins act as the glue that keeps the hair structure together. Replicine Functional Keratin™ technology understands and respects this difference and isolates each of these types of keratins separately. For example, some Replicine products incorporate keratin intermediate filament proteins. When applied to hair, these proteins repair hair strength by rebuilding damaged keratin intermediate filaments within the fibre. Other keratin technologies cannot distinguish between these different keratin types and treat all family members as one.
Maintain form and therefore function
Keratin protein structure is essential to physical and biological function. The Replicine Functional Keratin technology can keep large fibrous proteins intact, using them without breaking important bonds within the protein. These large molecular weight proteins can then be used to build tough structures, such as protective films on a hair fibre surface, wound care membranes or biodegradable plastics. Other keratin technologies often use only hydrolysis, breaking important bonds within the protein and losing the ability of the protein to build tough structures.
The amino acids in keratins are linked in a particular sequence. Within keratin materials, such as hair and skin, these sequences coil together like small bundles of rope, to build strong protein networks. The particular amino acids in the coil link, like teeth in a zipper, to lock the structure in place.
We have identified the specific amino acid sequences needed for this zipper effect, and ensured that they are maintained in our Replicine keratin proteins. The same sequences are present in human hair and so Replicine proteins can be considered hair identical proteins. Other keratin technologies break up amino acids, and so loose the important "teeth in the zipper" needed for good binding, essential for genuine hair repair.
Control the sulfur amino acids
Keratin proteins are characterized by the highest content of the sulfur amino acid cystine of any protein source, 3-10 times higher than the next most abundant protein source.
Cystine and sulfur metabolism is essential in the body for physical and biological performance, from giving the body the essential building blocks of glutathione, the body's weapon of choice to protect each and every cell from oxidative stress, to crosslinking keratin structures such as healthy strong nails.
Replicine Functional Keratin technology protects and controls the amino acid cystine to ensure it is available to the body to link to physical structures, or support the cell's biological pathways. Other keratin technologies destroy the amino acid cystine in an effort to make keratin soluble.
Core to the development of the Replicine Functional Keratin technology are the principles of scientific research, an evidence base for our product performance and associated publication of our results.
