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Peer-reviewedCC BY-NC-ND 4.0Biopolymers

Designed Protein‐Based Physical Crosslinker for Triple Helical Collagen Biomaterials

  • Amanda de Souza1,2
  • Gustavo Oliva Amaral1,2
  • Chuanbao Zheng2
  • Robbert Jan de Haas2
  • Marcelo Assis3
  • Ana Claudia Muniz Renno1
  • Renko de Vries2
  1. 1Department of Biosciences Federal University of São Paulo (UNIFESP) Santos SP Brazil
  2. 2Physical Chemistry and Soft Matter Wageningen University & Research Wageningen WE the Netherlands
  3. 3Institute of Advanced Marine Studies (IEAMar) São Paulo State University (UNESP) São Vicente SP Brazil
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Abstract

Collagen plays a pivotal role in animal body structure, but hydrogels of reconstituted collagens often have poor mechanical performance. Chemical crosslinking or the addition of other biopolymers are often used as a remedy. Inspired by the many natural collagen‐interacting proteins that modify the mechanics of collagen hydrogels, we explore protein‐based physical crosslinking of collagen as a route to modulate the mechanics of collagen hydrogels. A protein‐based crosslinker for collagen was designed based on an adhesion domain from Staphylococcus aureus . A tetramerization domain was coupled to an elastin‐like polypeptide as a spacer, followed by the collagen adhesion domain, yielding a tetrafunctional crosslinking. Circular Dichroism spectroscopy shows that the crosslinker has the expected secondary structure. Using quartz crystal microbalance, we demonstrate the tetrameric crosslinker binds rat tail Collagen I and fish collagen, even though the latter is largely denatured as evidenced by circular dichroism spectroscopy. Rheometry shows strong enhancement of elastic moduli and strain‐stiffening for rat tail collagen hydrogels, but smaller effects on the reduced fish collagen. Because CNA35 recognizes the collagen triple helix, this contrast indicates that the crosslinker acts specifically on triple‐helical collagen, and points to the importance of improved extraction protocols for alternative collagens that preserve native triple‐helical conformations.

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Cite

BibTeXRIS
BibTeX
@article{souza2026designed,
  title = {{Designed Protein‐Based Physical Crosslinker for Triple Helical Collagen Biomaterials}},
  author = {Amanda de Souza and Gustavo Oliva Amaral and Chuanbao Zheng and Robbert Jan de Haas and Marcelo Assis and Ana Claudia Muniz Renno and Renko de Vries},
  journal = {Biopolymers},
  year = {2026},
  month = oct,
  doi = {10.1002/bip.70129},
  url = {https://doi.org/10.1002/bip.70129},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Designed Protein‐Based Physical Crosslinker for Triple Helical Collagen Biomaterials
AU  - Amanda de Souza
AU  - Gustavo Oliva Amaral
AU  - Chuanbao Zheng
AU  - Robbert Jan de Haas
AU  - Marcelo Assis
AU  - Ana Claudia Muniz Renno
AU  - Renko de Vries
PY  - 2026
DA  - 2026/10/25
JO  - Biopolymers
DO  - 10.1002/bip.70129
UR  - https://doi.org/10.1002/bip.70129
AB  - Collagen plays a pivotal role in animal body structure, but hydrogels of reconstituted collagens often have poor mechanical performance. Chemical crosslinking or the addition of other biopolymers are often used as a remedy. Inspired by the many natural collagen‐interacting proteins that modify the mechanics of collagen hydrogels, we explore protein‐based physical crosslinking of collagen as a route to modulate the mechanics of collagen hydrogels. A protein‐based crosslinker for collagen was designed based on an adhesion domain from Staphylococcus aureus . A tetramerization domain was coupled to an elastin‐like polypeptide as a spacer, followed by the collagen adhesion domain, yielding a tetrafunctional crosslinking. Circular Dichroism spectroscopy shows that the crosslinker has the expected secondary structure. Using quartz crystal microbalance, we demonstrate the tetrameric crosslinker binds rat tail Collagen I and fish collagen, even though the latter is largely denatured as evidenced by circular dichroism spectroscopy. Rheometry shows strong enhancement of elastic moduli and strain‐stiffening for rat tail collagen hydrogels, but smaller effects on the reduced fish collagen. Because CNA35 recognizes the collagen triple helix, this contrast indicates that the crosslinker acts specifically on triple‐helical collagen, and points to the importance of improved extraction protocols for alternative collagens that preserve native triple‐helical conformations.
SN  - 0006-3525
SN  - 1097-0282
ER  -