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Dental Materials Journal Jul 2021We evaluated the influence of monomer type, plasticizer content, and powder/liquid (P/L) ratio on the setting characteristics of light-cured acrylic permanent soft...
Influence of monomer type, plasticizer content, and powder/liquid ratio on setting characteristics of acrylic permanent soft denture liners based on poly(ethyl methacrylate/butyl methacrylate) and acetyl tributyl citrate.
We evaluated the influence of monomer type, plasticizer content, and powder/liquid (P/L) ratio on the setting characteristics of light-cured acrylic permanent soft denture liners based on poly(ethyl methacrylate/butyl methacrylate). Two monomers, iso-butyl methacrylate (i-BMA) and 2-ethylhexyl methacrylate (2-EHMA), that contained various concentrations of the plasticizer acetyl tributyl citrate (ATBC) and trace amounts of the photo initiator and reducing agent were used. The P/L ratio was 1.0 or 1.2. The gelation time was measured using a controlled stress rheometer. Materials with i-BMA had shorter gelation times than those for materials with 2-EHMA. The gelation time increased exponentially with increasing plasticizer content. A higher P/L ratio led to a shorter gelation time. The effects of monomer type and plasticizer content were larger than that for the P/L ratio. These results show that 2-EHMA is a suitable monomer for soft denture liners and that the setting characteristics can be controlled via ATBC content.
Topics: Citrates; Denture Liners; Materials Testing; Methacrylates; Plasticizers; Powders
PubMed: 33814534
DOI: 10.4012/dmj.2020-319 -
Dental Materials Journal Jan 2018The aim of this study was to evaluate the amount of leached residual monomers from self-adhesive resin cements and evaluate their toxicity in-vitro. A total of 60...
The aim of this study was to evaluate the amount of leached residual monomers from self-adhesive resin cements and evaluate their toxicity in-vitro. A total of 60 disk-shaped specimens (5 mm in diameter and 0.5 mm in thickness) were prepared from each cement (RelyX U200, SpeedCEM, G-Cem) (n=20). Specimens were immersed in artificial saliva and the amount of released monomers [urethane dimethacrylate (UDMA) and triethyleneglycol dimethacrylate (TEGDMA)] was identified. Then, the cytotoxicity and genotoxicity effect on cells were evaluated using the defined amounts of released monomers from cements. The highest monomer release was detected in G-Cem (p<0.05). The highest cytotoxicity value was identified from SpeedCEM (p<0.01) and the highest genotoxicity values were calculated from RelyX U200 (p<0.05). Released UDMA and TEGDMA from self-adhesive resin cements induced cytotoxicity and genotoxicity effect on cells.
Topics: In Vitro Techniques; Materials Testing; Methacrylates; Polyethylene Glycols; Polymethacrylic Acids; Polyurethanes; Resin Cements; Saliva, Artificial
PubMed: 29225277
DOI: 10.4012/dmj.2016-380 -
Frontiers in Pharmacology 2023Atherosclerosis is the leading cause of numerous cardiovascular diseases with a high mortality rate. Non-coding RNAs (ncRNAs), RNA molecules that do not encode proteins... (Review)
Review
Atherosclerosis is the leading cause of numerous cardiovascular diseases with a high mortality rate. Non-coding RNAs (ncRNAs), RNA molecules that do not encode proteins in human genome transcripts, are known to play crucial roles in various physiological and pathological processes. Recently, researches on the regulation of atherosclerosis by ncRNAs, mainly including microRNAs, long non-coding RNAs, and circular RNAs, have gradually become a hot topic. Traditional Chinese medicine has been proved to be effective in treating cardiovascular diseases in China for a long time, and its active monomers have been found to target a variety of atherosclerosis-related ncRNAs. These active monomers of traditional Chinese medicine hold great potential as drugs for the treatment of atherosclerosis. Here, we summarized current advancement of the molecular pathways by which ncRNAs regulate atherosclerosis and mainly highlighted the mechanisms of traditional Chinese medicine monomers in regulating atherosclerosis through targeting ncRNAs.
PubMed: 38026969
DOI: 10.3389/fphar.2023.1283494 -
Life (Basel, Switzerland) Oct 2022(1) Background: This study aimed to examine the effect of bleaching agents on the release of triethylenae glycol dimethacrylate, 2-hydroxyethyl methacrylate, bisphenol...
(1) Background: This study aimed to examine the effect of bleaching agents on the release of triethylenae glycol dimethacrylate, 2-hydroxyethyl methacrylate, bisphenol A, urethane dimethacrylate, and bisphenol A-glycidyl methacrylate monomers, which are released from different composite resins, using the high-performance liquid chromatography (HPLC) method. (2) Methods: Ninety disc-shaped specimens were produced and immersed in artificial saliva. After different bleaching applications [office type bleaching (OB) and home type bleaching (HB)], the specimens were immersed in a 75 wt% ethanol/water solution, and the released monomers were analyzed by HPLC at predefined time intervals: 1, 7, and 28 days. The Kruskal−Wallis and Mann−Whitney U tests were conducted for statistical analysis (p = 0.05). (3) Results: The monomers were released at all times from all composite specimens. The monomer release was increased over time. The highest monomer release was detected on day 28. Bleaching applications affected monomer release. No statistical difference was found between OB and HB applications (p > 0.05). The most released monomer was Bisphenol-A in all composites. (4) Conclusion: Given that a residual monomer release from composite resins has a toxic effect and that bleaching treatments increase this release, a treatment protocol should be made in accordance with the manufacturer’s instructions.
PubMed: 36362868
DOI: 10.3390/life12111713 -
ACS Omega Jun 2020The Re(I) dimer complex, [(CO)(phen)Re1-(py)COORe2(phen)(CO)] (py = pyridine; phen = 1,10-phenanthroline), contains two different Re(I) centers 9.3 Å apart, one with a...
The Re(I) dimer complex, [(CO)(phen)Re1-(py)COORe2(phen)(CO)] (py = pyridine; phen = 1,10-phenanthroline), contains two different Re(I) centers 9.3 Å apart, one with a nitrogen donor and the other with an acetate donor from the bridging isonicotinate ligand. The complexes were characterized by H NMR, UV-vis, fluorescence, and IR spectroscopy, elemental analysis, and single-crystal X-ray diffraction. The absorption and emission properties of the dimer dominated by charge transfer transitions are analyzed with respect to those of the monomers, [(CO)(phen)Re-N(pyCOOCH)] and [(CO)(phen)ReOOCCH]. Spectral comparison of these three complexes results in the unexpected finding that the dimer emission (575 nm) occurs near that of the nicotinate-containing monomer (580 nm) rather than near the lower energy-emitting state (650 nm) of the acetate-containing monomer. Density functional theory (DFT) calculations elucidate this unusual emission behavior. The geometries of the dimer and two monomers are optimized in the singlet ground and lowest-energy triplet excited states (LLTS's) to interpret absorption and emission behaviors, respectively. The singlet excited states calculated using time-dependent DFT correlate well with the absorption spectra in the lowest-energy and other major electronic transitions. The energy gaps and low-lying singlet excited states of the dimer are close to those of the acetate-containing monomer. The lowest-energy Franck-Condon triplet excited state of the dimer arising from electronic transitions localized on the acetate moiety is unstable. The next higher Franck-Condon triplet excited state arises from long-range charge transfer transition, and its energy is close to that of the nicotinate-containing monomer. Optimization of the dimer LLTS yields a stable state based on a long-range charge transfer transition involving occupied orbitals partially localized on the bridging nicotinate moiety. The LLTS energies of the dimer and nicotinate-containing monomer are in very good agreement as are the emission energies of these complexes. The correlated spectroscopic and computational results corroborate to the understanding of charge transfer states and transitions toward the development of photosensitive compounds for photoelectrochemical solar energy conversion cells.
PubMed: 32548478
DOI: 10.1021/acsomega.0c00704 -
Molecules (Basel, Switzerland) Jun 2023Photodynamic therapy (PDT) is recognized as a powerful method to inactivate cells. However, the photosensitizer (PS), a key component of PDT, has suffered from undesired...
Photodynamic therapy (PDT) is recognized as a powerful method to inactivate cells. However, the photosensitizer (PS), a key component of PDT, has suffered from undesired photobleaching. Photobleaching reduces reactive oxygen species (ROS) yields, leading to the compromise of and even the loss of the photodynamic effect of the PS. Therefore, much effort has been devoted to minimizing photobleaching in order to ensure that there is no loss of photodynamic efficacy. Here, we report that a type of PS aggregate showed neither photobleaching nor photodynamic action. Upon direct contact with bacteria, the PS aggregate was found to fall apart into PS monomers and thus possessed photodynamic inactivation against bacteria. Interestingly, the disassembly of the bound PS aggregate in the presence of bacteria was intensified by illumination, generating more PS monomers and leading to an enhanced antibacterial photodynamic effect. This demonstrated that on a bacterial surface, the PS aggregate photo-inactivated bacteria via PS monomer during irradiation, where the photodynamic efficiency was retained without photobleaching. Further mechanistic studies showed that PS monomers disrupted bacterial membranes and affected the expression of genes related to cell wall synthesis, bacterial membrane integrity, and oxidative stress. The results obtained here are applicable to other types of PSs in PDT.
Topics: Organometallic Compounds; Zinc Compounds; Photosensitizing Agents; Isoindoles; Photobleaching; Photochemotherapy; Escherichia coli; Staphylococcus aureus
PubMed: 37375194
DOI: 10.3390/molecules28124639 -
Foods (Basel, Switzerland) Sep 2023The development of packaging technology has become a crucial part of the food industry in today's modern societies, which are characterized by technological... (Review)
Review
The development of packaging technology has become a crucial part of the food industry in today's modern societies, which are characterized by technological advancements, industrialization, densely populated cities, and scientific advancements that have increased food production over the past 50 years despite the lack of agricultural land. Various types of food-packaging materials are utilized, with plastic being the most versatile. However, there are certain concerns with regards to the usage of plastic packaging because of unreacted monomers' potential migration from the polymer packaging to the food. The magnitude of monomer migration depends on numerous aspects, including the monomer chemistry, type of plastic packaging, physical-chemical parameters such as the temperature and pH, and food chemistry. The major concern for the presence of packaging monomers in food is that some monomers are endocrine-disrupting compounds (EDCs) with a capability to interfere with the functioning of vital hormonal systems in the human body. For this reason, different countries have resolved to enforce guidelines and regulations for packaging monomers in food. Additionally, many countries have introduced migration testing procedures and safe limits for packaging monomer migration into food. However, to date, several research studies have reported levels of monomer migration above the set migration limits due to leaching from the food-packaging materials into the food. This raises concerns regarding possible health effects on consumers. This paper provides a critical review on plastic food-contact materials' monomer migration, including that from biodegradable plastic packaging, the monomer migration mechanisms, the monomer migration chemistry, the key factors that affect the migration process, and the associated potential EDC human health risks linked to monomers' presence in food. The aim is to contribute to the existing knowledge and understanding of plastic food-packaging monomer migration.
PubMed: 37761073
DOI: 10.3390/foods12183364 -
Frontiers in Cell and Developmental... 2021The liver-derived plasma protein fetuin A is a systemic inhibitor of ectopic calcification. Fetuin-A stabilizes calcium phosphate mineral initially as ion clusters to...
BACKGROUND
The liver-derived plasma protein fetuin A is a systemic inhibitor of ectopic calcification. Fetuin-A stabilizes calcium phosphate mineral initially as ion clusters to form calciprotein monomers (CPM), and then as larger multimeric consolidations containing amorphous calcium phosphate (primary CPP, CPP 1) or more crystalline phases (secondary CPP, CPP 2). CPM and CPP mediate excess mineral stabilization, transport and clearance from circulation.
METHODS
We injected i.v. synthetic fluorescent CPM and studied their clearance by live two-photon microscopy. We analyzed organ sections by fluorescence microscopy to assess CPM distribution. We studied cellular clearance and cytotoxicity by flow cytometry and live/dead staining, respectively, in cultured macrophages, liver sinusoidal endothelial cells (LSEC), and human proximal tubule epithelial HK-2 cells. Inflammasome activation was scored in macrophages. Fetuin A monomer and CPM charge were analyzed by ion exchange chromatography.
RESULTS
Live mice cleared CPP in the liver as published previously. In contrast, CPM were filtered by kidney glomeruli into the Bowman space and the proximal tubules, suggesting tubular excretion of CPM-bound calcium phosphate and reabsorption of fetuin A. Fetuin-A monomer clearance was negligible in liver and low in kidney. Anion exchange chromatography revealed that fetuin A monomer was negatively charged, whereas CPM appeared neutral, suggesting electrochemical selectivity of CPM versus fetuin A. CPM were non-toxic in any of the investigated cell types, whereas CPP 1 were cytotoxic. Unlike CPP, CPM also did not activate the inflammasome.
CONCLUSIONS
Fetuin-A prevents calcium phosphate precipitation by forming CPM, which transform into CPP. Unlike CPP, CPM do not trigger inflammation. CPM are readily cleared in the kidneys, suggesting CPM as a physiological transporter of excess calcium and phosphate. Upon prolonged circulation, e.g., in chronic kidney disease, CPM will coalesce and form CPP, which cannot be cleared by the kidney, but will be endocytosed by liver sinusoidal endothelial cells and macrophages. Large amounts of CPP trigger inflammation. Chronic CPM and CPP clearance deficiency thus cause calcification by CPP deposition in blood vessels and soft tissues, as well as inflammation.
PubMed: 33996793
DOI: 10.3389/fcell.2021.633925 -
Designed Monomers and Polymers 2017Smart system employed CO gas as new trigger has been attracting enormous attention in recent years, but few monomers that are capable of switching their...
Smart system employed CO gas as new trigger has been attracting enormous attention in recent years, but few monomers that are capable of switching their hydrophobicity/hydrophility upon CO stimulation have been reported. A novel CO responsive monomer, 4-vinylbenzyl amidine, is designed and synthesized in this work with -dimethylacetamide dimethyl acetal and 4-vinylbenzyl amine that is prepared through the Gabriel reaction. In bi-phase solvent of -hexane and water, the monomer dissolves in -hexane first and then transforms into water upon the CO treatment, indicating a hydrophobic to hydrophilic transition. This transformation is demonstrated as reversible by monitoring the conductivity variation of its wet dimethyl formamide solution during alternate bubbling/removing CO. The protonation of 4-vinylbenzyl amidine upon CO treatment is demonstrated by H NMR which also accounts for the dissolubility change. The reversible addition-fragmentation chain-transfer polymerization of this monomer is also performed, finding the reaction only occurs in glacial acetic acid. The reason can be ascribed to the different radical structure produced in different solvent.
PubMed: 29491807
DOI: 10.1080/15685551.2016.1270027 -
The Journal of Biological Chemistry Jun 2019Tubulin, the subunit of microtubules, is a noncovalent heterodimer composed of one α- and one β-tubulin monomer. Both tubulins are encoded by multiple genes or...
Tubulin, the subunit of microtubules, is a noncovalent heterodimer composed of one α- and one β-tubulin monomer. Both tubulins are encoded by multiple genes or composed of different isotypes, which are differentially expressed in different tissues and in development. Tubulin αβ dimers are found throughout the eukaryotes and, although very similar, are known to differ among organisms. We seek to investigate tubulins from different tissues and different organisms for a basic physical characteristic: heterodimer stability and monomer exchange between heterodimers. We previously showed that mammalian brain tubulin heterodimers reversibly dissociate, following the mass action law. Dissociation yields native monomers that can exchange with added tubulin to form new heterodimers. Here, we compared the dissociation of tubulins from multiple sources, including mammalian (rat) brain, cultured human cells (HeLa cells), chicken brain, chicken erythrocytes, and the protozoan We used fluorescence-detected analytical ultracentrifugation to measure tubulin dissociation over a >1000-fold range in concentration and found that tubulin heterodimers from different biological sources differ in by as much as 150-fold under the same conditions. Furthermore, when fluorescent tracer tubulins from various sources were titrated with unlabeled tubulin from a single source (rat brain tubulin), heterologous dimerization occurred, exhibiting similar affinities, in some cases binding even more strongly than with autologous tubulin. These results provide additional insight into the regulation of heterodimer formation of tubulin from different biological sources, revealing that monomer exchange appears to contribute to the sorting of α- and β-tubulin monomers that associate following tubulin folding.
Topics: Amino Acid Sequence; Animals; Brain; Chickens; Erythrocytes; Humans; Leishmania; Models, Molecular; Protein Conformation; Protein Multimerization; Rats; Sequence Homology; Tubulin
PubMed: 31110044
DOI: 10.1074/jbc.RA119.007973