Recombinant Human Collagen Type I / COL1

Dai, Xiaomei, et al. Biomaterials Advances 158 (2024): 213799.

Type I collagen (COL1), the primary structural protein in the extracellular matrix of tendons and bone, plays a pivotal role in the development of biomimetic materials for regenerative medicine. This study demonstrates the application of COL1 in the fabrication of a dual-phase, gradient composite scaffold designed to repair tendon–bone interface injuries—a clinical challenge due to the poor healing capacity of this transitional tissue.

A bilayer scaffold was engineered using COL1 and hydroxyapatite (HAp) powders, each blended with 10% gelatin and stirred separately to form uniform mixtures. The HAp layer was first cast and set at 4 °C, followed by the addition of the COL1 layer. After sequential cooling, the scaffold underwent chemical cross-linking using either Genipin, EDC/NHS, or a dual cross-linking strategy to enhance structural integrity and biological performance.

The optimal scaffold—dual cross-linked COL1/HAp—was loaded with human amniotic mesenchymal stem cells (hAMSCs) and implanted in a rat rotator cuff injury model. Micro-CT, histological, and biomechanical analyses confirmed superior healing, including aligned collagen fibers, fibrocartilage formation, and improved mechanical strength at 12 weeks post-implantation.

This work highlights the critical role of COL1 in scaffold design and provides a viable strategy for enhancing tendon–bone interface healing through biomimetic materials combined with stem cell therapy.

Poomrattanangoon, Sasiprapa, and Dakrong Pissuwan. Nanoscale Advances 7.12 (2025): 3867-3880.

Type I collagen was employed as a functional coating for gold nanorods (GNRs) to create a bioactive nanocomposite (GNRs@C) with enhanced wound healing potential. In this study, the biocompatibility and cellular uptake of GNRs were significantly improved by surface conjugation with type I collagen, enabling effective interaction with human skin fibroblast (HSF) cells.

GNRs were synthesized via a seed-mediated growth method and subsequently modified with poly(sodium 4-styrenesulfonate) (PSS) before conjugation with type I collagen. The GNRs@C nanocomposite, when combined with light-emitting diode (LED) irradiation, significantly promoted HSF cell proliferation and accelerated scratch wound closure. Notably, full closure of scratched HSF monolayers was observed within 40 hours under GNRs@C and LED treatment, compared to untreated controls.

In addition to its wound-closure efficacy, the treatment substantially reduced inflammatory cytokines, including IL-6 and TNF-α, while upregulating key angiogenic and regenerative factors such as VEGF and bFGF. These biological responses underscore the synergistic effects of collagen-functionalized nanomaterials and photothermal stimulation in tissue repair.

This case highlights the critical role of type I collagen as a biologically active stabilizer and functional ligand in nanomaterial-based wound healing platforms, offering a promising strategy for non-invasive, photothermally enhanced regenerative therapies.

Vrehen, Annika F., et al. Materials Today Bio 26 (2024): 101021.

Collagen type I is a critical structural protein in the human corneal stroma. In a recent study, two peptide analogues—UPy-GFOGER and UPy-DGEA—were synthesized to mimic collagen type I for incorporation into supramolecular hydrogels. The GFOGER sequence (GGG-GPP₅-GFOGER-GPP₅), rich in glycine-proline-proline (GPP) repeats, was designed to promote triple-helix formation, a hallmark of natural collagen. In contrast, DGEA (GCGDGEA) lacks this structural complexity.

The peptides were conjugated with ureido-pyrimidinone (UPy) moieties and embedded in a UPy-based hydrogel system composed of UPy-Glycine and UPy-PEG₁₀K-UPy. These hydrogels were used to encapsulate primary human corneal keratocytes (PKs), enabling comparative assessment of peptide-induced bioactivity.

Structural analysis confirmed that UPy-GFOGER self-assembled into nanofibers with triple-helical superstructure, whereas UPy-DGEA remained structurally simple. Biologically, UPy-GFOGER hydrogels supported PK elongation and redifferentiation, indicating effective mimicry of native extracellular matrix cues. In contrast, UPy-DGEA led to minimal cell spreading, highlighting its limited biofunctionality.

This study demonstrates that collagen type I mimicking GFOGER peptide, when integrated into a supramolecular hydrogel, enables advanced 3D culture environments by promoting keratocyte differentiation. Its structured assembly and bioactivity underscore the importance of triple-helical motifs for replicating native collagen behavior in biomaterial design.