Understanding Collagen Fibrillogenesis and Their Role in Skin Health

As we age, the collagen fibrils in our skin begin to break down and become disorganized, contributing to the visible signs of aging. While boosting collagen is often emphasized, healthy collagen fibril formation is even more crucial for preserving youthful-looking skin.

Collagen, a protein produced by animal cells, is rich in specific amino acids. These collagen molecules assemble into fibrils of 10-500 nanometers.

Fibril structures vary significantly; they may be thin and transparent, as found in the cornea, or thick and bundled, as seen in tendons. The arrangement and properties of these fibrils are crucial to their functions.

Collagen molecules can self-organize into fibrils. However, without guidance from the cell, this process results in a random gel that lacks the specific orientation and structure required for functional tissues.

To produce functional fibrils and tissues, cells secrete not only collagen but also various signaling proteins to guide the fibril formation process, also known as collagen fibrillogenesis.

Listed below are examples of signaling proteins produced by cells that are important for skin health.

Decorin: Enhancing Collagen Assembly

Decorin binds to collagen fibrils, promoting their proper alignment and organization. Studies have shown that Decorin-deficient mice suffer from fragile skin, highlighting its importance in maintaining skin strength and resilience. The presence of Decorin ensures that collagen fibrils are correctly assembled, contributing to the skin’s structural integrity.

Fibulin: Catalyzing Cross-Linking

Fibulin supports copper ion transfer, which is a critical step in the elastin-collagen cross-linking process. This cross-linking is vital for the formation of strong and elastic fibers in connective tissues. Research has demonstrated that Fibulin-deficient mice often die of artery and diaphragmatic rupture due to disrupted collagen and elastic fiber formation.

Lumican: Regulating Collagen Fibril Growth

Lumican ensures that collagen fibrils grow at a controlled rate, preventing abnormalities in their size and structure. Lumican-deficient mice exhibit skin laxity and corneal opacity, conditions arising from deregulated growth of collagen fibrils that result in abnormally thick collagen fibrils. By controlling the growth of collagen fibrils, Lumican plays a critical role in maintaining the proper structure and function of tissues.

Connective Tissue Growth Factor (CTGF): Promoting Collagen Production

CTGF stimulates fibroblasts to produce collagen, supporting tissue repair and regeneration. The balanced secretion of CTGF ensures that collagen production is sufficient for tissue maintenance and repair without leading to adverse effects.

Aging and acute UVB exposure reduce Fibulin and CTGF production, making topical replenishment of these proteins an effective way to support skin health.

“Cell-Identical Multi-Peptides” Biotechnology

Cells produce hundreds of signaling proteins in precise amounts and proportions to ensure proper function.

While these proteins aren’t available from plants and are challenging to extract from animal tissues, advances in biotechnology have made it possible to produce them by replicating the cellular biological process.

The Zellulin® BioPlatform, for instance, uses patented technology to cultivate cells from a single fish, producing these signaling proteins in a sustainable and traceable manner. These proteins are then transformed into biopeptide complexes that can significantly improve skin hydration, elasticity, firmness and dermal density.

Produced by the Zellulin® BioPlatform, ZelluGEN™, is a biopeptide complex that encourages skin cells to produce more and stronger extracellular matrix, the structural foundation of the skin. ZelluGEN™ is proven to help renew, protect, and maintain youthful skin and is suitable for use in advanced anti-aging formulations.

 

Manufacturer
Avant Proteins Pte. Ltd.
Unit No. 06-03, Tee Yih Jia Food Hub
5 Senoko Road,
Singapore 758137

Contact
sales@zellulin.tech
+65 8758 0863

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¹ Richard W. Loo et al., “In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen”, JOVE September 20th, 2012
² Keith M. Meek et al., “Structural control of corneal transparency, refractive power and dynamics”, Eye Volume 39, p 644-50 February 2024
³ Prasad Sawadkar et al., “Development of a surgically optimized graft insertion suture technique to accommodate a tissue-engineered tendon in vivo”, Biores Open Access Volume 2, Issue5, p.327-35 October 2013
⁴ Suzanne E.G. Fligiel et al., “Collagen Degradation in Aged/Photodamaged Skin In Vivo and After Exposure to Matrix Metalloproteinase-1 In Vitro”, JID Volume 120, Issue 5, p.842-848 May 2003