Defective chicken skin collagen molecules, hydrolyzed by actinidain protease, assemble to form loosely packed fibrils that promote cell spheroid formation.

Cells recognize collagen fibrils as the first step in the process of adherence. Fibrils of chicken skin actinidain-hydrolyzed collagen (low adhesive scaffold collagen, LASCol), in which the telopeptide domains are almost completely removed, cause adhering cells to form spheroids instead of adopting a monolayer morphology. Our goal was to elucidate the ultrastructure of the LASCol fibrils compared with pepsin-hydrolyzed collagen (PepCol) fibrils. At low concentration of 0.2 mg/mL, the time to reach the maximum increasing rate of turbidity for LASCol was all slower than that for PepCol. Differential scanning calorimetry showed that the thermal stability of collagen self-assembly changed significantly between pH 5.5 and pH 6.6 with and without a small number of telopeptides. However, the calorimetric enthalpy change did not vary much in that pH range. The melting temperature of LASCol fibrils at pH 7.3 was 55.1 °C, whereas PepCol fibrils exhibited a peak around 56.9 °C. The D-periodicity of each fibril was the same at 67 nm. Nevertheless, the looseness of molecular packing in LASCol fibrils was demonstrated by circular dichroism measurements and immuno-scanning electron microscopy with a polyclonal antibody against type I collagen. As there is a close relationship between function and structure, loosely packed collagen fibrils would be one factor that promotes cell spheroid formation. Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.

Citation

Koichi Morimoto, Saori Kunii, Ben'ichiro Tonomura. Defective chicken skin collagen molecules, hydrolyzed by actinidain protease, assemble to form loosely packed fibrils that promote cell spheroid formation. International journal of biological macromolecules. 2021 Jan 15;167:1066-1075

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PMID: 33220378

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