50 SUSTAINABILITY
homology between their amino acid sequence and that of human collagen. The amino acid sequence of vegan collagen developed by fermentation technology can be 100% homologous with human body. However, it should be emphasized that not
all vegan collagen from fermentation sources on the market is 100% homologous, depending on the specific production technology and amino acid sequence measurement. Studies have shown that the existence of non-human collagen amino acid sequences (i.e., tag amino acids) will affect the triple helix structure of proteins, and then affect cell migration, proliferation, differentiation and so on.1
There are many fermentable vegan collagen
sources on the market, but their sequences vary widely. Due to process limitations, they are first
labeled with amino acids for easy purification and are not removed from the final product. Furthermore, it is not ruled out that some vegan collagen with tag amino acids from fermented sources is less safe and effective than animal collagen. Therefore, 100% homology with human collagen, also known as type A humanized collagen in China, is a key direction for future development.
Efficacy mechanism study Collagen is the main component of the extracellular matrix (ECM), which plays an important role in skin repair and scar formation. There is usually a good dynamic balance between collagen synthesis and degradation in ECM. However, excessive synthesis, insufficient
degradation and disorderly accumulation of collagen can lead to tissue fibrosis or pathological scar formation, affecting its normal function or completely losing its function. The abnormal expression of collagen directly
affects the surrounding environment of cells, thus inducing a series of abnormal cell activities and inducing the mass production of cytokines and signaling molecules. Studies on the mechanism of collagen in the skin also have a lot to explore. For example, the distribution of collagen such as collagen I, collagen III, collagen IV, collagen VI, collagen XII, collagen XIV and collagen XVI in different skin layers is different. Collagen I, collagen III and collagen V are
dermal collagen, collagen IV, collagen VII and collagen XVII are basement membrane collagen,
Figure 2: High power stereoscopic observation of self-assembly of collagen III fibres by cryo-ET. The coloured part is collagen fibre with a diameter of about 100nm
and these collagen may affect telomeres, or cellular energy such as ATP and affect the metabolism of cells such as fibroblasts, keratinocytes, melanocytes and macrophages. Collagen I and collagen III are familiar to us, these two kinds of collagen can bind to cells through integrins, which in turn affect cell activity. Fragments of collagen III also have
certain functions, such as promoting collagen regeneration as follows. Collagen IV is synthesized by fibroblasts and
epidermal cells, and can be distributed in all connective tissues.2
It is a major component of
the dermal and epidermal junction of the skin, with a small distribution in the dermal papillary layer, but hardly detectable in the dermal reticular layer. Some studies indicate that collagen IV can
activate and promote the secretion of matrix metalloproteinase-9 (MMP-9) and matrix metalloproteinase-2 (MMP-2).3
MMP-9 can
degrade many ECM components, especially collagen, which plays an important role in tissue remodeling. However, both MMP-2 and 9 can degrade forming many voids in the
collagen IV,4
basement membrane, facilitating the migration of activated interstitial fibroblasts, and aggravating tissue fibrosis through the release of collagen I and III. In addition, collagen IV has dual effects on
wound healing. On the one hand, it participates in the formation of basement membrane, and makes the epidermis adhere to the papillary
dermis to promote wound healing. On the other hand, it can inhibit the adhesion of vascular endothelial cells to the vascular basement membrane, prevent the formation of new blood vessels, and delay wound healing. For collagen VI, it can form microfibril to
promote the deposition of collagen I and collagen III, promote cell adhesion, and activate the activity of matrix metalloproteinases to reshape wound tissue and promote wound healing. In addition, other studies have shown
that collagen VI may have growth factor-like properties,5
and it may be one of the extracellular
matrix molecules that are first digested and released by proteases during inflammation or remoulding. These released collagen VI fragments, as an autocrine or paracrine medium, can promote mitosis of interstitial cells and rapidly repair wounds. Among them, collagen XVII, which targets
the stem cell (epidermal stem cell, hair follicle stem cell, melanin stem cell) niche, has an excellent role in skin ageing and wound repair.6 Furthermore, hair follicle stem cells provide a functional niche for melanocyte stem cells.7 At the same time, according to literature collagen XVII also has a certain role
reports,8
in preventing hair loss. Local injection of 2mg/ ml collagen XVII fragment can promote the hair growth of AGA model mice, and the combined injection of 2mg/ml collagen III fragment has a more significant effect. Activation of Wnt signaling pathway may be
Figure 3: Artificial intelligence screening of collagen core functional region PERSONAL CARE October 2024
www.personalcaremagazine.com
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