Differential impact of the triple helix dissociation degree of collagen on the binding efficiency with cancer cells and normal cells

Abstract

Collagen plays a crucial role in cancer development and migration. However, the impact of changes in the collagen molecular structure on its interaction with cancer cells remains unclear. In this study, natural bovine tendon collagen was heat-treated to obtain collagen samples with different triple helix dissociation degrees. Three methods, including cell adhesion assay, fluorescence labeling assay, and cancer cell capture assay, were employed to compare the binding efficiency of collagen samples to both breast cancer cells (MCF-7) and human umbilicus vein endothelial cells (HUVECs). The results demonstrated that collagen samples exhibited stronger binding efficiency to cancer cells than to normal cells. Additionally, untreated collagen samples showed higher cell binding efficiency compared to heat-treated collagen samples. Furthermore, by comparing the differences in the binding efficiency of collagen samples with different triple helix dissociation degrees to cancer cells and normal cells, it was confirmed that untreated collagen samples exhibited the greatest disparity in binding efficiency with both cell types. Moreover, a strong linear relationship was observed between the triple helix dissociation degree of collagen and the capture rate of cancer cells in the co-culture system. These findings provide important insights into the role of collagen in cancer development.