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Ground type-I collagen—a focused study on its fibrillogenesis behavior and bioactivity in vitro

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Abstract

Take bovine tendon type-I collagen as the raw material, we pretreated it by freezing and then grinding the macromolecule at a low temperature (4–10 °C). Effects of the grinding process on the molecular structure, water solubility, fibrillogenesis behavior in vitro and biological activity of collagen were systematically prospected. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) results revealed that the collagen had typical structural characteristics of type-I collagen; moreover, grinding treatment gave rise to partially degraded collagen molecules which took on continuous bands with lower molecular weights different from α1 and α2. More strikingly, the degradation degree positively corresponded to the grinding duration. Circular dichroism (CD) analysis manifested that with extended grinding, intensities of both the positive and negative peaks for collagen samples shrunk. Interestingly, grinding also contributed to improved water solubility of collagen. The water solubility of the sample ground for 20 min (COL20) was 1.91 mg/mL, which is about 6 times higher than that of the natural collagen sample (0.28 mg/mL). Amid the study concerning the fibrillogenesis behavior, turbidity and rheological data collaboratively demonstrated that with prolonged grinding time, the assembly rate and degree of the sample plunged. Assembled gel from the ground collagen with finer fibrils was also observed in scanning electron microscope (SEM), which further embraced the conclusion aforementioned in fibrillogenesis kinetics. Cell experiments corroborated that the grinding process can be harnessed to manipulate the cell proliferation promoting ability of collagen. Simultaneously, further dissection of COL20 with the best biological activity clarified that the water-soluble part and water-insoluble part of COL20 had distinct aptitudes as to promoting cell proliferation as well as inhibiting the growth of liver cancer cells.

Graphical abstract

Cryogrinding treatment, which may give rise to physical and chemical changes of substances out of its prominent mechanical force on specimens, was utilized to modulate performances of collagen, including its water solubility, gel properties and biological capacities. The resultant collagen powder with improved water solubility and bioactivity is expected to expedite its actual processing and applications.

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Availability of data and materials

The data sets generated during and/or analysed during the current study are available from the corresponding author on reasonable request.

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Acknowledgements

This study was supported by the National Natural Science Foundation of China (No. 22178277).

Funding

National Natural Science Foundation of China, 22178277, haibo wang.

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Author notes

  1. Yuling Xu, Haibo Wang, and Lang He have equally contributed to this work.

Authors and Affiliations

  1. School of Chemical and Environmental Engineering, Wuhan Polytechnic University, Wuhan, 430074, Hubei, People’s Republic of China

    Yuling Xu, Lei Dai, Ke Li, Jialin Liu, Haibo Wang, Lang He, Chengzhi Xu, Benmei Wei & Juntao Zhang

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  1. Yuling Xu
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  2. Lei Dai
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  3. Ke Li
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  4. Jialin Liu
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  7. Chengzhi Xu
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Contributions

YX, LH, HW: conceptualization, methodology, software; LD, KL: data curation, writing—original draft preparation; JL, LD: visualization, investigation; CX, BW: supervision; JZ: software, validation, writing—reviewing and editing.

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Correspondence to Haibo Wang or Lang He.

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Xu, Y., Dai, L., Li, K. et al. Ground type-I collagen—a focused study on its fibrillogenesis behavior and bioactivity in vitro. Macromol. Res. 31, 75–83 (2023). https://doi.org/10.1007/s13233-022-00108-3

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  • DOI: https://doi.org/10.1007/s13233-022-00108-3

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