Poly(acrylic acid)-Assisted Intrafibrillar Mineralization of Type I Collagen: A Review

The mineralization of type I collagen is a biological process occurring in vertebrates by which some hard tissues such as bone and dentin are constructed. Due to the extensive clinical needs for bone defect repair and remineralization of mineral-depleted dentin, biomimetic mineralization of collagen is attracting more and more interests. Synthetic analogs of noncollagenous proteins are necessary for directing the in vitro mineralization. In this paper, the function and mechanism of poly(acrylic acid) (PAA) in regulating the mineralization, especially intrafibrillar mineralization (IM) of collagen are reviewed. As two mineralization patterns (extrafibrillar and intrafibrillar) co-exist in natural hard tissues, differences between them in terms of microstructure, biodegradation, cytocompatibility, osteoinduction in vitro, and performance in vivo are systematically compared. Then the roles of PAA in biomimetic collagen IM within one-analog and two-analog systems are discussed, respectively. Moreover, mineralization of some self-mineralizable collagen matrices is described. Due to the interactions between collagen and PAA play a crucial role in the processes of collagen mineralization, some reference researches are also provided involving the collagen/PAA interactions in some other fields. Finally, this review is ended with an outlook for future potential improvements based on the collection of existing bottlenecks in this field.

Automated summary

This review discusses the function and mechanism of poly(acrylic acid) (PAA) in regulating the mineralization of collagen, particularly intrafibrillar mineralization (IM). The differences between two mineralization patterns (extrafibrillar and intrafibrillar) in terms of microstructure, biodegradation, cytocompatibility, osteoinduction in vitro, and performance in vivo are systematically compared. The review also includes the mineralization of self-mineralizable collagen matrices and references regarding collagen/PAA interactions in other fields. Finally, future potential improvements in this field are discussed.