Abstract
Front Cover: The interest in collagen mineralization has increased in recent years because it allows producing biomimetic bone like structures. The authors present a base-acid neutralization method to self-assemble and mineralize type I collagen with different extent of apatite concentration, mimicking osteochondral structures, and doped with luminescent Tb3+ for bioimaging applications. The mineralized fibrils, and especially those Tb3+-doped, induce osteogenic differentiation of human mesenchymal stem cells. This is reported by Ismael Romero-Castillo, Elena López-Ruiz, Jorge Fernando Fernández-Sánchez, Juan Antonio Marchal, and Jaime Gómez-Morales in article number 2000319.
Highlights
Type-I collagen (Col) is the most abundant structural protein in mammals
We studied the cytocompatibility of the samples and their ability to induce osteogenic differentiation of human mesenchymal stem cells
The X-ray diffraction (XRD) patterns of samples prepared by the base-acid titration variant at reagent concentrations C1, C2, C3 and Col/calcium phosphate (CaP) ratios 50:50, 70:30 and 90:10 are shown in Figure 1 (a-c)
Summary
Type-I collagen (Col) is the most abundant structural protein in mammals. It can be found in tendon and epithelial tissues, as well as in bone and teeth, where plays a structural role as an extracellular protein, and determine their mechanical and elastic behaviour. [1,2]Bone is a mineralized tissue with particular hierarchical architecture, mechanical properties and remodeling capabilities.[2]. Type-I collagen (Col) is the most abundant structural protein in mammals. It can be found in tendon and epithelial tissues, as well as in bone and teeth, where plays a structural role as an extracellular protein, and determine their mechanical and elastic behaviour. Bone is a mineralized tissue with particular hierarchical architecture, mechanical properties and remodeling capabilities.[2] The basic building unit of the intimate structure of the bone is a self–assembled collagen fibril, mainly type I collagen, mineralized with apatite nanocrystals at both intrafibrillar and interfibrillar zones.[3,4,5,6] Type I collagen is a trimeric molecule that consist of two 1 and one 2 peptide chains, formed by a repetitive sequence of glycine–X–Y, with X and Y being normally proline and hydroxyproline residues. The interaction between tropocollagen units leads to the formation of fibrillar structures with a regular array of gaps and overlap spaces, observed in transmission electron microscopy (TEM) as a periodic banding pattern of 67 nm (D-spacing).[3,4,5,6] The mineral component is a poorly crystalline, non-stoichiometric Ca2+– and OH–deficient apatite -the stoichiometric hydroxyapatite (HA) is Ca10(PO4)6(OH)2-, coated with citrate and doped with 4– 6 wt % of carbonate, 0.9 wt% Na, 0.5 wt% Mg and others minor elements.[7,8]
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