Engineered dual affinity protein fragments to bind collagen and capture growth factors
Open accessAbstract
Collagen type I lacks affinity for growth factors (GFs) and yet it is clinically used to deliver bone morphogenic protein 2 (BMP-2), a potent osteogenic growth factor. To mitigate this lack of affinity, supra-physiological concentrations of BMP-2 are loaded in collagen sponges leading to uncontrolled BMP-2 leakage out of the material. This has led to important adverse side effects such as carcinogenesis. Here, we design recombinant dual affinity protein fragments, produced in E. Coli, which contain two regions, one that spontaneously binds to collagen and a second one that binds BMP-2. By adding the fragment to collagen sponges, BMP-2 is sequestered enabling solid phase presentation of BMP-2. We demonstrate osteogenesis in vivo with ultra-low doses of BMP-2. Our protein technology enhances the biological activity of collagen without using complex chemistries or changing the manufacturing of the base material and so opens a pathway to clinical translation.
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In vivo studies using animal bone defect models demonstrate that PDA-functionalized scaffolds exhibit pronounced bone regeneration capability.
“In vivo studies using animal bone defect models have demonstrated that such PDA-functionalized scaffolds exhibit pronounced bone regeneration capability, highlighting their potential as alternative therapeutic strategies in maxillofacial reconstructive surgery.”
From Polydopamine-Based Biomaterials in Oral Medicine: Applications, Mechanisms, and Translational Challenges (2026) · cites this paper as [34]
The Results section reports bone formation in a mouse forearm defect model, supporting the in vivo bone-regeneration aspect of the claim. But the tested scaffolds were collagen sponges treated with a dual-affinity protein fragment and rhBMP-2, not PDA-functionalized scaffolds; our copy does not establish their use for maxillofacial reconstruction. (LLM, conf=0.86)
Experimental — accuracy not yet measuredWithin porous scaffold architectures, PDA deposition improves surface hydrophilicity and cytocompatibility and functions as a mineralization template facilitating apatite nucleation and deposition, and incorporation of PDA nanoparticles into hydrogel matrices markedly enhances their mechanical properties, tissue adhesive strength, and osteogenic activity.
“Within porous scaffold architectures, PDA deposition not only improves surface hydrophilicity and cytocompatibility but also functions as an effective mineralization template, facilitating apatite nucleation and deposition and thereby establishing a biomimetic microenvironment conducive to bone tissue regeneration.”
From Polydopamine-Based Biomaterials in Oral Medicine: Applications, Mechanisms, and Translational Challenges (2026) · cites this paper as [34]
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- Authors
- Sarrigiannidis, S. O., Dobre, O., Navarro, A. R., Dalby, M. J., Gonzalez-Garcia, C., & Salmeron-Sanchez, M.
- Affiliations
- University of Glasgow (GB)
- Venue
- Materials Today Bio
- Publisher
- Elsevier BV
- Published
- 2023-06
- Volume
- 20
- Pages
- 100641
- ISSN
- 2590-0064 (ISSN-L)
- PMC
- PMC10173277
- OpenAlex
- W4366748226
- Cited by
- 6
- References
- 39
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2
- FWCI
- 0.47
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Materials Today Bio (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion, cc-by-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Engineering and Physical Sciences Research Council (EP/P001114/1)
- Medical Research Scotland
- UK Regenerative Medicine Platform
- UKRI Medical Research Council (MR/R015651/1)
- Topics
- Physical Sciences › Engineering › Biomedical Engineering › Bone Tissue Engineering Materials
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- type I collagen, BMP-2, BMP-2 delivery, growth factor sequestration, collagen-binding protein, collagen sponge, bone formation, recombinant protein engineering, bone tissue engineering
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