Current cosmetic development is moving toward molecularly defined actives with greater structural precision. In this context, recombinant type III collagen is positioned as one of the most advanced solutions to address skin aging from a structural perspective.

For decades, collagen has been a common ingredient in cosmetic formulations due to its fundamental role in the extracellular matrix. However, biotechnological innovation has made it possible to overcome the limitations of traditional collagen, leading to recombinant peptides with greater functional specificity, improved bioavailability, and high batch-to-batch reproducibility.

MicoreCol® III Pro represents this new generation: a peptide derived from human type III collagen, obtained through fermentation, with 100% homology to the native human sequence.

Type III collagen: a key component of the dermis

Type III collagen is an essential fibrillar collagen in the dermis, where it contributes to the formation of microfibrillar networks that regulate elasticity and the three-dimensional organization of the extracellular matrix. Its presence is particularly high in young skin, where it actively supports the structural cohesion of the tissue.

While type I collagen provides tensile strength, type III plays a key role in dermal flexibility, tissue remodeling, and repair processes. The functional balance between both subtypes is critical for maintaining firmness and elasticity.

With aging, the progressive decline of type III collagen disrupts fibrillar architecture, reduces dermal density, and promotes the appearance of wrinkles and loss of firmness.

Limitations of conventional collagen in cosmetics

Traditionally, collagen used in cosmetics has been derived from animal sources such as bovine, porcine, or marine tissue. While these forms have shown efficacy as film-forming and moisturizing agents, their biological functionality presents structural limitations.

The inherent variability of animal-derived tissues can affect batch-to-batch consistency and ingredient purity, creating challenges in terms of standardization and traceability. In addition, their high molecular weight limits penetration beyond the stratum corneum, restricting their activity to a superficial moisturizing and protective effect.

To address the deeper mechanisms of skin aging, it is necessary to move toward molecules with optimized size, defined structure, and a real capacity to interact with dermal cells.

Application of biotechnology in the development of recombinant human collagen

Recombinant human collagen developed by Jinbo Bio-Pharmaceutical is obtained through fermentation systems based on Escherichia coli, enabling precise control of the amino acid sequence and high industrial reproducibility.

This approach offers clear advantages:

  • 100% homology with human collagen
  • Removal of tag sequences that may interfere with conformational structure
  • High purity
  • Sustainable and scalable production
  • Vegan profile aligned with ethical trends

Development focuses on the structural analysis of the full human collagen sequence to identify domains with optimized cellular interaction capacity.

MicoreCol III Pro: Selection of an active functional fragment

Using advanced structural modeling tools and sequence analysis, multiple regions of human type III collagen were evaluated to identify a domain with high functional potential located within a specific region of the protein.

The selected region exhibits features that are highly relevant from both structural and functional perspectives. Its sequence includes triplets rich in charged amino acids, a characteristic pattern of collagen that promotes cellular recognition. This organization allows it to maintain a stable triple-helix conformation, a hallmark of human collagen that is essential for preserving its biological activity.

In addition, the fragment exhibits a solubility profile suitable for incorporation into cosmetic formulations, facilitating homogeneous dispersion and compatibility with different formulation systems. At an industrial level, its size and structural stability enable controlled and reproducible production through fermentation, ensuring batch-to-batch consistency and scalability.

The result is a small recombinant peptide (approximately 3 kDa) that retains the characteristic triple-helix structure of human collagen. This triple helix exhibits a slight curvature, promoting a more adaptable spatial arrangement.

Rather than being an irrelevant structural detail, this configuration facilitates its accommodation within the cellular environment and enhances its ability to interact with receptors on the cell surface.

Cell adhesion: enhanced interaction with the extracellular matrix

Studies show that MicoreCol® III Pro significantly enhances cellular adhesion capacity. In comparative assays, its activity was 1.83 times higher than that of type I collagen.

This effect is mediated by integrins, receptors located on the cell surface that regulate the interaction between cells and the extracellular matrix. Enhanced adhesion promotes more efficient interaction with the dermal environment, a key factor in maintaining structural organization and tissue functionality.

Transdermal penetration: functional in vitro evidence

One of the main challenges of topical collagen is its penetration. In Franz diffusion models, MicoreCol® III Pro showed progressive, time-dependent absorption:

  • 33% at 4 hours
  • 70% at 8 hours
  • 86% at 12 hours

In vivo efficacy: measurable improvement in skin parameters

In a 28-day clinical study with a serum formulated with 0.2% MicoreCol® III Pro, significant improvements were observed compared to the control group.

  • 9.23% reduction in nasolabial fold length
  • 10.61% reduction in average depth
  • 22.04% increase in skin firmness
  • 16.04% reduction in roughness
  • 12.77% increase in epidermal density

The increase in firmness and density supports an effect at the level of dermal structure and the extracellular matrix.

Strategic differentiation in the European cosmetic market

The European cosmetic market is evolving toward development models grounded in evidence, quality control, and industrial sustainability. Ingredient traceability and consistency between mechanism of action and measurable outcomes have become key factors in decision-making.

In this context, MicoreCol® III Pro provides structural precision, human homology, and experimental validation—key elements that reinforce its positioning as a differentiated ingredient in next-generation anti-aging formulations.

MicoreCol® III Pro is part of the biotechnological portfolio of Ismael Quesada Personal Care in the Spanish market, within its line of biotechnology-derived actives.

References:

  • HUA, Chen, et al. Characterization by high-resolution crystal structure analysis of a triplehelix region of human collagen type III with potent cell adhesion activity. Biochemical and
    biophysical research communications, 2019, vol. 508, no 4, p. 1018-1023 https://pubmed.ncbi.nlm.nih.gov/30545625/

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