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The potential of salivary albumin to degrade composite resin.
Acta Odontol Latinoam
April 2023
Sao Leopoldo Mandic Research Institute, División of Cariology and Restorative Dentistry, Campiñas, Brazil.
Unlabelled: Albumin is a salivary enzyme capable of cleaving ester linkages and catalyzing degradation of resin-based dental materials. However, the effect of concentration-dependent esterolytic action on composite resins as yet remains unexplored.
Aim: The purpose of this study was to evaluate whether artificial saliva formulations with different concentrations of albumin affected the surface roughness, flexural strength and microhardness of a composite resin.
Biodegradation Studies of Novel Fluorinated Di-Vinyl Urethane Monomers and Interaction of Biological Elements with Their Polymerized Films.
Polymers (Basel)
August 2017
Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, ON M5G 1M1, Canada.
The monomeric components of resin composites in dental restorative materials are susceptible to hydrolysis in the oral cavity. The main objective of this study was to assess the bio-stability of fluorinated urethane dimethacrylates and determine the nature of fluoro-chemistry interactions with protein and bacterial adhesion (both sources of hydrolytic activity) onto cured resin. Degradation studies were performed in the presence of either albumin (in a mildly alkaline pH) or cholesterol esterase (CE).
View Article and Find Full Text PDFDry powder pulmonary delivery of cationic PGA-co-PDL nanoparticles with surface adsorbed model protein.
Int J Pharm
August 2015
Formulation and Drug Delivery Research, School of Pharmacy and Biomolecular Sciences, Liverpool John Moores University, Liverpool, United Kingdom. Electronic address:
Pulmonary delivery of macromolecules has been the focus of attention as an alternate route of delivery with benefits such as; large surface area, thin alveolar epithelium, rapid absorption and extensive vasculature. In this study, a model protein, bovine serum albumin (BSA) was adsorbed onto cationic PGA-co-PDL polymeric nanoparticles (NPs) prepared by a single emulsion solvent evaporation method using a cationic surfactant didodecyldimethylammonium bromide (DMAB) at 2% w/w (particle size: 128.64±06.
View Article and Find Full Text PDFBiodegradation of composite resin with ester linkages: identifying human salivary enzyme activity with a potential role in the esterolytic process.
Dent Mater
August 2014
Faculty of Dentistry, University of Toronto, ON, Canada; Institute of Biomedical and Biomaterials Engineering, University of Toronto, ON, Canada; Materials Science Engineering, University of Toronto, ON, Canada. Electronic address:
Objectives: The ester linkages contained within dental resin monomers (such as Bisphenol A-glycidylmethacrylate (BisGMA) and triethylene glycol dimethacrylate (TEGDMA)) are susceptible to hydrolytic degradation by salivary esterases, however very little is known about the specific esterase activities implicated in this process. The objective of this work was to isolate and identify the dominant proteins from saliva that are associated with the esterase activities shown to be involved in the degradation of BisGMA.
Methods: Human whole saliva was collected and processed prior to separation in a HiPrep 16/60 Sephacryl S-200 HR column.
Photocrosslinked bovine serum albumin hydrogels with partial retention of esterase activity.
Enzyme Microb Technol
February 2012
Institute of Pharmaceutical Science, School of Biomedical & Health Sciences, King's College London, 150 Stamford Street, London SE1 9NH, United Kingdom.
Novel biohybrid hydrogels based on bovine serum albumin (BSA) were synthesized by one-pot photopolymerization of chemically modified protein in the presence of N,N'-methylenebisacrylamide (MBA) as cross-linking agent under mild conditions. Two batches of methacrylated albumins were prepared by treating the protein with different amounts of methacrylic anhydride (MAN) and the degree of substitution (DS) of primary amines was quantified via trinitrobenzesulfonic acid (TNBS) colorimetric assay. Hydrogels readily formed when a diluted buffered solution of the modified protein and MBA was exposed to LW-UV in the presence of 1-[4-(2-hydroxyethoxy)phenyl]-2-hydroxy-2-methyl-1-propan-1-one (Irgacure 2959) as the radical initiator.
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