Enzyme-assisted mineralization of calcium phosphate: exploring confinement for the design of highly crystalline nano-objects

Colaço, Elodie; Lefèvre, Damien; Maisonhaute, Emmanuel; Brouri, Dalil; Guibert, Clément de; Dupont-Gillain, Christine; Kirat, Karim El; Demoustier‐Champagne, Sophie; Landoulsi, Jessem

doi:10.1039/d0nr01638a

Cited by 19 publications

(16 citation statements)

References 60 publications

(68 reference statements)

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“…The emergence of in vitro enzyme-assisted mineralization has motivated material scientists to explore ALP for the design of CaP-based materials with outstanding mechanical properties and bioactivity [120][121][122][123]. [118]). (B) Mechanism of the enzymatic process (adapted from [117]).…”

Section: Figure 3 (A)mentioning

confidence: 99%

“…In a recent article [ 118 ], we immobilized ALP enzymes within a multilayered film, using the sequential LbL technique, and showed the possibility to initiate CaP mineralization on the solid surface. Moreover, by combining real-time monitoring and ex situ characterization techniques, we observed that the growth mechanism of the mineral was significantly impacted by the physicochemical conditions of the medium (pH and temperature).…”

Section: Enzymatic Approachmentioning

confidence: 99%

“…Recently, we reported the successful immobilization of ALP on the wall of a nanoporous track-etched template using LbL assembly and their subsequent mineralization. This led to the formation of CaP particles along the nanopore wall at different surface coverages and with different morphologies and crystallinities depending on the main factors influencing this process (mineralization time, pH, temperature) [ 118 ]. Various results were found for these systems, highlighting the role of the confined generation of orthophosphate to form CaP minerals along the nanopore walls, yielding mineralized nanotube/nanowire objects.…”

Section: Enzymatic Approachmentioning

confidence: 99%

“… ( A ) Three-dimensional structure of ALP (PDB, code “P19111”). Different views showing the dimensions of the homodimer and the distribution of the superimposed residues, Glu (in blue) and Asp (in red) amino acids (adapted from [ 118 ]). ( B ) Mechanism of the enzymatic process (adapted from [ 117 ]).…”

Section: Figurementioning

confidence: 99%

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Enzymatic Approach in Calcium Phosphate Biomineralization: A Contribution to Reconcile the Physicochemical with the Physiological View

Guibert

Landoulsi

2021

IJMS

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Biomineralization is the process by which organisms produce hard inorganic matter from soft tissues with outstanding control of mineral deposition in time and space. For this purpose, organisms deploy a sophisticated “toolkit” that has resulted in significant evolutionary innovations, for which calcium phosphate (CaP) is the biomineral selected for the skeleton of vertebrates. While CaP mineral formation in aqueous media can be investigated by studying thermodynamics and kinetics of phase transitions in supersaturated solutions, biogenic mineralization requires coping with the inherent complexity of biological systems. This mainly includes compartmentalization and homeostatic processes used by organisms to regulate key physiological factors, including temperature, pH and ion concentration. A detailed analysis of the literature shows the emergence of two main views describing the mechanism of CaP biomineralization. The first one, more dedicated to the study of in vivo systems and supported by researchers in physiology, often involves matrix vesicles (MVs). The second one, more investigated by the physicochemistry community, involves collagen intrafibrillar mineralization particularly through in vitro acellular models. Herein, we show that there is an obvious need in the biological systems to control both where and when the mineral forms through an in-depth survey of the mechanism of CaP mineralization. This necessity could gather both communities of physiologists and physicochemists under a common interest for an enzymatic approach to better describe CaP biomineralization. Both homogeneous and heterogeneous enzymatic catalyses are conceivable for these systems, and a few preliminary promising results on CaP mineralization for both types of enzymatic catalysis are reported in this work. Through them, we aim to describe the relevance of our point of view and the likely findings that could be obtained when adding an enzymatic approach to the already rich and creative research field dealing with CaP mineralization. This complementary approach could lead to a better understanding of the biomineralization mechanism and inspire the biomimetic design of new materials.

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Section: Figure 3 (A)mentioning

confidence: 99%

Section: Enzymatic Approachmentioning

confidence: 99%

Section: Enzymatic Approachmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Enzymatic Approach in Calcium Phosphate Biomineralization: A Contribution to Reconcile the Physicochemical with the Physiological View

Guibert

Landoulsi

2021

IJMS

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“…This idea has motivated the use of enzymes for the development of biomimetic systems, which may help to better understand the mechanism of biomineralization, , or for the design of biomaterials. − In recent works, we have used tissue nonspecific alkaline phosphatase (ALP, EC 3.1.3.1) to initiate CaP mineralization in the homogeneous phase by generating, in situ, orthophosphate ions, which precipitate in the presence of calcium ions . This procedure was also successfully applied on solid surfaces, using immobilized enzymes, resulting in the formation of nanostructured mineralized layers . Interestingly, we observed that the degree of confinement influences the crystal phase.…”

Section: Introductionmentioning

confidence: 99%

Embedding Collagen in Multilayers for Enzyme-Assisted Mineralization: A Promising Way to Direct Crystallization in Confinement

et al. 2021

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The biogenic calcium phosphate (CaP) crystallization is a process that offers elegant materials design strategies to achieve bioactive and biomechanical challenges. Indeed, many biomimetic approaches have been developed for this process in order to produce mineralized structures with controlled crystallinity and shape. Herein, we propose an advanced biomimetic approach for the design of ordered hybrid mineralized nano-objects with highly anisotropic features. For this purpose, we explore the combination of three key concepts in biomineralization that provide a unique environment to control CaP nucleation and growth: (i) self-assembly and self-organization of biomacromolecules, (ii) enzymatic heterogeneous catalysis, and (iii) mineralization in confinement. We use track-etched templates that display a high density of aligned monodisperse pores so that each nanopore may serve as a miniaturized mineralization bioreactor. We enhance the control of the crystallization in these systems by coassembling type I collagen and enzymes within the nanopores, which allows us to tune the main characteristics of the mineralized nano-objects. Indeed, the synergy between the gradual release of one of the mineral ion precursors by the enzyme and the role of the collagen in the regulation of the mineralization allowed to control their morphology, chemical composition, crystal phase, and mechanical stability. Moreover, we provide clear insight into the prominent role of collagen in the mineralization process in confinement. In the absence of collagen, the fraction of crystalline nano-objects increases to the detriment of amorphous ones when increasing the degree of confinement. By contrast, the presence of collagen-based multilayers disturbs the influence of confinement on the mineralization: platelet-like crystalline hydroxyapatite form, independently of the degree of confinement. This suggests that the incorporation of collagen is an efficient way to supplement the lack of confinement while reinforcing mechanical stability to the highly anisotropic materials. From a bioengineering perspective, this biomineralization-inspired approach opens up new horizons for the design of anisotropic mineralized nano-objects that are highly sought after to develop biomaterials or tend to replicate the complex structure of native mineralized extracellular matrices.

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Self‐Activating Phosphorus‐Rich Substrate Import Enzyme Catalytic Domains for Bone Regeneration

Zhao,

Chen,

Tang

et al. 2024

Adv Funct Materials

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Enzymes play a key role in natural mineralization, but their function is disabling in bone metabolism when patients suffer severe degenerations like hypophosphatasia. To regulate bone homeostasis, a self‐activating phosphorus‐rich system is proposed on calcium glycerophosphate (CaGP) modified polyurethane (PU) fibrous substrate, wherein ample enzyme catalytic domains are imported with intestinal alkaline phosphatase (IALP) chelating and activating by calcium in situ that is testified by chemical potential evaluation. Therefore, Ca‐bonding IALP catalyzes organophosphate to phosphate locally to achieve a calcified symbiotic state, regulating mineralization and accelerating osteoinduction in vitro and in vivo. The self‐activating enzyme system promotes early osteogenic differentiation and angiogenesis, resulting in rapid healing of cranial defect with a “long‐tail” effect compared to an enzyme‐assisted system. Transcriptomic and metabolomic analyses demonstrate positive associations with neovascularization and calcium/phosphorus metabolism, specifically upregulated glycerophospholipids and calcium ions in favor of osteogenic differentiation under cytokine‐free conditions. These results provide a potential enzyme‐activating therapy in bone homeostasis and regeneration.

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Enzyme-assisted mineralization of calcium phosphate: exploring confinement for the design of highly crystalline nano-objects

Abstract: Calcium phosphate mineralization is initiated through heterogenous enzymatic catalysis, resulting in the formation of highly ordered anisotropic nanostructures. The mineral phase features are modulated by physicochemical factors and confinement.

Cited by 19 publications

References 60 publications

Enzymatic Approach in Calcium Phosphate Biomineralization: A Contribution to Reconcile the Physicochemical with the Physiological View

Enzymatic Approach in Calcium Phosphate Biomineralization: A Contribution to Reconcile the Physicochemical with the Physiological View

Embedding Collagen in Multilayers for Enzyme-Assisted Mineralization: A Promising Way to Direct Crystallization in Confinement

Self‐Activating Phosphorus‐Rich Substrate Import Enzyme Catalytic Domains for Bone Regeneration

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