BIOTECHNOLOGIES
The beauty of biodesign: new frontier for collagen
Dr Paul Mouser, Erin Turner, Michela Caffrey, Dr Nick Ouzounov - Geltor
Today’s beauty consumer demands sustainable, animal-free, and performance driven products. These shifting sentiments put active ingredients in the spotlight and demand innovation. Biodesign is rising to the challenge. This approach to product development combines advances in computational biology and precision fermentation to deliver the best of nature’s depth and diversity to consumers. While many are familiar with biotechnology’s first breakthrough ingredient – hyaluronic acid (HA) – proteins like collagen have rapidly emerged as the pioneering products enabled by biodesign. HA from microbial fermentation paved the
way for future fermentation-derived bioactive ingredients. In 1998 scientists at Savient Pharmaceuticals successfully produced high molecular weight HA, historically sourced from rooster combs, through precision fermentation of the microorganism Streptococcus zooepidemicus.1 Biotechnology unlocked the potential to create sustainable alternatives to animal-derived molecules that eliminate unethical practices, complicated supply chains, and the use of environmentally harsh chemical processes. Collagen is another popular ingredient in
beauty and an important target for biodesign as it is the most abundant protein in the human body, responsible for structure, stability, and strength within the dermal layers. In addition to its essential structural function, collagen is a signaling molecule defining cellular activities. There are at least 28 types of collagen
identified in the body, all sharing a common triple helix structure yet differing in a- chain composition. These differences offer unique properties. The
fibrillar collagens, types I and III, constitute over 90% of collagen content within the skin and are major determinants of the strength and stiffness of the tissue. Although the minor collagens make up less than 10% of the total collagen content, they play a key role in extracellular matrix (ECM) organisation, such as formation and anchoring of the basement membrane, regulation of fibrillar collagen assembly, and mediating growth factor and cell signaling.2 The name collagen is derived from the Greek
word ‘kolla’, which means glue, and the suffix ‘-gono’, signifying producer. Interest in collagen originated in Asia. During the Tang Dynasty (618- 907), for example, imperial consort Yang Yuhuan was considered one of China’s great beauties. Opting for anti-ageing remedies, she regularly consumed soup containing collagen from donkey
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hide, known as Eijao, believing it would keep her skin glowing and youthful.3 Labeled as a ‘fountain of youth’, most
collagen for consumer products is animal derived, using harsh chemical treatments to separate the ingredient from cowhide, bone, or pigskin, without consideration for biocompatibility with human skin. Animal collagen is also associated with adverse allergic or immunogenic reactions, batch-to-batch variability, unpleasant odours, colour and purity issues, and potential transmission of diseases or pathogens. Additionally, there may be religious constraints for porcine and bovine-sourced collagen, contradicting inclusive positioning for beauty products. Skin ageing is characterized by three features:
atrophy of the dermis due to loss of collagen, degeneration in the elastic fibre network, and loss of hydration. Therefore, maintaining the integrity of the skin’s ECM is important to conserve a youthful appearance. Reduction of fibrillar (types I and III) collagen is a key characteristic feature of chronologically aged skin and is enhanced in photodamage.4 A sustained down-regulation in collagen
synthesis is observed in photodamaged skin compared to healthy sun-protected skin,5
in chronologically aged, sun-protected skin compared to young skin.6
and The changes of collagen
in ageing skin are a result of decreased fibroblast proliferation with decreased production of new collagen in conjunction with an increased production of matrix metalloproteinases.
naturally decreases approximately 1%-1.5% per year.7
With age, the ability to replenish collagen This decrease in collagen is one of the
characteristic hallmarks associated with the appearance of fine lines and deeper wrinkles. Collagen solutions have recently begun
shifting away from being entirely animal-based. This accelerating change can be traced to Geltor’s development of a proprietary biodesign platform and their introduction of the world’s first biodesigned collagen product portfolio. One area of focus has been delivering bioactive collagens based on the properties of collagen type 21, and the company has delivered two solutions to-date based on this work: ■ HumaColl21®, a biomimetic human Type 21 collagen for beauty and wellness ■ PrimaColl®, a Type 21 collagen for food and nutrition. Type 21 is a rare collagen making up less than
1% of the total collagen in the body. Like other collagens, native production of type 21 decreases into adulthood.8
Type 21 is a FACIT collagen
(fibril-associated collagens with interrupted triple helices) which is known to function as a molecular bridge between other collagens and a cell messenger.9
Unlike more abundant
types, it is difficult to isolate and extract from conventional sources and can only be accessed as an ingredient through biodesign. HumaColl21, hereafter known as H21, is
biodesigned to be an exact match to the functional core region of collagen type 21, resulting in a low molecular weight bioactive
March 2023 PERSONAL CARE
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