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Production and Functional Analysis of Collagen Hexapeptide Repeat Sequences in Pichia pastoris
Ist Teil von
Journal of agricultural and food chemistry, 2024-05, Vol.72 (24), p.13622-13633
Ort / Verlag
United States: American Chemical Society
Erscheinungsjahr
2024
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
In the development of biomaterials with specific structural domains associated with various cellular activities, the limited integrin specificity of commonly used adhesion sequences, such as the RGD tripeptide, has resulted in an inability to precisely control cellular responses. To overcome this limitation, we conducted multiple replications of the integrin α2β1-specific ligand, the collagen hexapeptide Gly-Phe-Pro-Gly-Glu-Arg (GFPGER) in Pichia pastoris. This enabled the development of recombinant collagen with high biological activity, which was subsequently expressed, isolated, and purified for structural and functional analysis. The proteins carrying the multiple replications GFPGER sequence demonstrated significant bioactivity in cells, leading to enhanced cell adhesion, osteoblast differentiation, and mineralization when compared to control groups. Importantly, these effects were mediated by integrin α2β1. The new collagen constructed in this study is expected to be a biomaterial for regulating specific cell functions and fates.