Publications by authors named "Mosser G"

Plant-derived natural bioactive molecules are of great therapeutic potential but, so far, their application in nanomedicine has scarcely been studied. This work aimed at comparing two methodologies, i.e.

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Standard cell cultures are one of the pillars of biomedical sciences. However, there is increasing evidence that 2D systems provide biological responses that are often in disagreement with observations, partially due to limitations in reproducing the native cellular microenvironment. 3D materials that are able to mimic the native cellular microenvironment to a greater extent tackle these limitations.

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Fibrin-Type I collagen composite gels have been widely studied as biomaterials, in which both networks are usually formed simultaneously at a neutral pH. Here, we describe a new protocol in which mixed concentrated solutions of collagen and fibrinogen were first incubated at acidic pH to induce fibrinogen gel formation, followed by a pH change to neutral inducing collagen fiber formation. Thrombin was then added to form fibrin-collagen networks.

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Cellulose nanocrystals (CNCs) have been widely studied as fillers to form reinforced nanocomposites with a wide range of applications, including the biomedical field. Here, we evaluated the possibility to combine them with fibrinogen and obtain fibrin hydrogels with improved mechanical stability as potential cellular scaffolds. In diluted conditions at a neutral pH, it was evidenced that fibrinogen could adsorb on CNCs in a two-step process, favoring their alignment under flow.

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The elaboration of scaffolds able to efficiently promote cell differentiation toward a given cell type remains challenging. Here, we engineered dense type I collagen threads with the aim of providing scaffolds with specific morphological and mechanical properties for C3H10T1/2 mesenchymal stem cells. Extrusion of pure collagen solutions at different concentrations (15, 30, and 60 mg/mL) in a PBS 5× buffer generated dense fibrillated collagen threads.

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Fibrin-based gels are used in clinics as biological glues but their application as 3D cellularized scaffolds is hindered by processing and stability issues. Silicification of fibrin networks appears as a promising strategy not only to address these limitations but also to take advantage of the bioactivity of Si. However, it raises the question of the influence of silica sources on fibrin self-assembly.

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A platform of enzymatically-crosslinked Collagen/Tyramine hyaluronan derivative (Col/HA-Tyr) hydrogels with tunable compositions and gelation conditions was developed to evaluate the impact of the preparation conditions on their physical, chemical and biological properties. At low HA-Tyr content, hydrogels exhibited a fibrillar structure, with lower mechanical properties compared to pure Col hydrogels. At high HA-Tyr and Horse Radish Peroxydase (HRP) content, a microfibrillar network was formed beside the banded Col fibrils and a synergistic effect of the hybrid structure on mechanical properties was observed.

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Type I collagen is the main component of the extracellular matrix (ECM). In vitro, under a narrow window of physicochemical conditions, type I collagen self-assembles to form complex supramolecular architectures reminiscent of those found in native ECM. Presently, a major challenge in collagen-based biomaterials is to couple the delicate collagen fibrillogenesis events with a controlled shaping process in non-denaturating conditions.

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Article Synopsis
  • The study focused on enhancing the organization and transparency of collagen scaffolds using lyotropic mesogen properties of collagen, achieving distinct liquid crystal phases with specific acid mixtures.
  • It was found that these collagen scaffolds showed varying visual properties, ranging from opaque to transparent, and had improved viscoelastic properties ideal for molding processes.
  • When tested on human corneal epithelial cells, the collagen matrices demonstrated superior biocompatibility and better amplification of limbal stem cells compared to amniotic membranes, highlighting their potential for use in ophthalmology.
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Collagen and its denatured form, gelatin, are biopolymers of fundamental interest in numerous fields ranging from living tissues to biomaterials, food, and cosmetics. This study aims at characterizing mixtures of those biopolymers at high concentrations (up to 100 mg·mL) at which collagen has mesogenic properties. We use a structural approach combining polarization-resolved multiphoton microscopy, polarized light microscopy, magnetic resonance imaging, and transmission electron microscopy to analyze gelatin and collagen/gelatin dense phases in their sol and gel states from the macroscopic to the microscopic scale.

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Tendon injury is a clinical, societal and economical issue. Moreover, tendon repair represents an important clinical challenge, partly due to the mechanical constraints that occur at the junctions with muscle and bone. Several strategies have been developed for tendon repair.

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This work aims at characterizing the three-dimensional organization of liquid crystals composed of collagen, in order to determine the physico-chemical conditions leading to highly organized structures found in biological tissues such as cornea. To that end, we use second-harmonic generation (SHG) microscopy, since aligned collagen structures have been shown to exhibit intrinsic SHG signals. We combine polarization-resolved SHG experiments (P-SHG) with the theoretical derivation of the SHG signal of collagen molecules tilted with respect to the focal plane.

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Cutaneous chronic wounds are characterized by an impaired wound healing which may lead to infection and amputation. When current treatments are not effective enough, the application of wound dressings is required. To date, no ideal biomaterial is available.

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Several diseases can lead to opacification of cornea requiring transplantation of donor tissue to restore vision. In this context, transparent collagen I fibrillated matrices have been synthesized at 15, 30, 60 and 90 mg/mL. The matrices were evaluated for fibril organizations, transparency, mechanical properties and ability to support corneal epithelial cell culture.

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In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar, and denatured states using one and two dimensional {(1)H}-(13)C solid-state NMR spectroscopy. We interpret (13)C chemical shift variations in terms of dihedral angle conformation changes.

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Bio-hybrid networks are designed based on the self-assembly of surface-engineered collagen-silica nanoparticles. Collagen triple helices can be confined on the surface of sulfonate-modified silica particles in a controlled manner. This gives rise to hybrid building blocks with well-defined diameters and surface potentials.

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We show by combining small-angle X-ray scattering (SAXS) and cryo-transmission electron microscopy (cryo-TEM) that anionic silica nanoparticles (SiNPs) assemble into well-defined 1D cluster when mixed with a dilute solution of semiflexible chitosan polycation. The nanorods are stable in excess of SiNPs and composed of 10 SiNPs well-ordered into straight single strands with length ≈ 184.0 nm and radius = 9.

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The recent booming of multiphoton imaging of collagen fibrils by means of second harmonic generation microscopy generates the need for the development and automation of quantitative methods for image analysis. Standard approaches sequentially analyse two-dimensional (2D) slices to gain knowledge on the spatial arrangement and dimension of the fibrils, whereas the reconstructed three-dimensional (3D) image yields better information about these characteristics. In this work, a 3D analysis method is proposed for second harmonic generation images of collagen fibrils, based on a recently developed 3D fibre quantification method.

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The long-term fate of fluorescent non-porous FITC-SiO(2) nanoparticles of various sizes (10-200 nm) and charge is studied in the presence of human dermal fibroblasts. Particle aggregates are formed in the culture medium and uptaken, at least partially, by macropinocytosis. The smallest particles have a strong impact on cell viability and genotoxic effects can be observed for negatively-charged colloids 10 nm in size.

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Hybrid and nanocomposite silica-collagen materials derived from concentrated collagen hydrogels were evaluated in vitro and in vivo to establish their potentialities for biological dressings. Silicification significantly improved the mechanical and thermal stability of the collagen network within the hybrid systems. Nanocomposites were found to favor the metabolic activity of immobilized human dermal fibroblasts while decreasing the hydrogel contraction.

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As the delivery of healthcare services increasingly emphasizes interprofessional activity, one major occupation, healthcare administration, is conspicuously absent from the discussion. This situation reflects the structure of healthcare delivery organizations as professional bureaucracies, with clinical professionals practicing with relative autonomy and with administrators viewed as quasi- or semi-professionals. Not only is this a missed opportunity for administrators, but it seriously weakens the potential for change and improvement promised by interprofessional practice.

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Normal collagen hydrogels, currently used as the dermal layer of skin substitute Apligraf®, are obtained by encapsulating dermal fibroblasts in a collagen hydrogel at low concentration (0.66 mg/ml). However they suffer from extensive contraction by cells and weak resistance against degradation, which limits their use as permanent graft.

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Silica-collagen bionanocomposite hydrogels were obtained by addition of silica nanoparticles to a protein suspension followed by neutralization. Electron microscopy studies indicated that larger silica nanoparticles (80 nm) do not interact strongly with collagen, whereas smaller ones (12 nm) form rosaries along the protein fibers. However, the composite network structurally evolved with time due to the contraction of the cells and the dissolution of the silica nanoparticles.

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