Effectiveness of Violet LED alone or in association with bleaching gel during dental photobleaching: A Systematic Review.

AIMS: To conduct a systematic review to determine the efficacy of violet led in promoting dental bleaching by itself or accelerating dental bleaching when associated with peroxides. METHODS: Clinical and in vitro studies were identified by a search on November 27th 2020 in the PubMed and Scopus databases. Inclusion criteria were: 1) studies related to bleaching; 2) studies related to violet LED Light (405-410nm); and 3) studies that analyzed efficacy. The authors assessed the studies for risk of bias independently. Authors extracted outcomes including color change evaluation and pain assessment independently. RESULTS: During the search process, 895 articles were found in the previously cited databases. After the first screening consisting of title and abstract evaluations, 18 articles were selected. Finally, 13 articles met the eligibility criteria and were included in this review, being 5 clinical trial/case series and 8 in vitro studies. In vitro studies showed a high risk of bias and interventional studies showed a low risk of bias. CONCLUSION: The violet Led seems to have the potential to bleach teeth without peroxides, with a clinical perceptible color alteration. However, the effect is small in comparison to bleaching using peroxides. When Violet Led is used in association with peroxides, it seems to potentialize the bleaching result. However, due to the high heterogeneity between studies, a small number of clinical studies, and the high risk of bias of the in vitro included studies, the results are not definitive, and further well-designed studies are needed to reach safe evidence.

Enzyme oxidation of plant galactomannans yielding biomaterials with novel properties and applications, including as delivery systems.

New biomaterials from renewable sources and the development of "functionalized biopolymers" are fields of growing industrial interest. Plant polysaccharides represent a valid alternative to traditional synthetic polymers, which are obtained from monomers of fossil, non-renewable origin. Several polysaccharides, either in their natural or chemically/biochemically modified forms, are currently employed in the biomedical, food and feed, and industrial fields, including packaging. Sustainable biochemical reactions, such as enzyme modifications of polysaccharides, open further possibilities for new product and process innovation. In the present review, we summarize the recent progress on enzyme oxidation of galactomannans (GM) from few leguminous plants (performed either with galactose oxidase or laccase) and we focus on the versatile and easily accessible laccase/TEMPO oxidative reaction. The latter causes a steep viscosity increase of GM water solutions and a transition of the gels from a viscous to an elastic form, due to formation of emiacetalic bonds and thus of internal cross-linking of the polymers. Following lyophilization of these hydrogels, stable aerogels can be obtained, which were shown to have good potential as delivery systems (DS) of actives. The active molecules tested and herewith described are polymyxin B, an antibiotic; nisin, an antimicrobial peptide; the enzymes lysozyme, protease and lipase; the mixture of the industrial microbiocides 5-chloro-2-methyl-4-isothiazolin-3-one (CIT) and 2-methyl-4-isothiazolin-3-one (MIT). The advantages of such aerogel systems and the possibilities they open for future developments, including as DS, are described.

Tooth color changes and sensitivity in patients undergoing dental bleaching with 10% hydrogen peroxide using customized trays or strips: a randomized clinical trial.

BACKGROUND: This paper aimed to compare the tooth color changes and sensitivity in patients undergoing dental bleaching with 10% hydrogen peroxide using customized trays or strips as delivering systems. METHODS: A total of 50 patients aged between 18-30 years old were assigned into two groups (N.=25) according to the bleaching treatment: tray (TB) or strips (SB). For both techniques, the patients underwent a 30-minute application of 10% hydrogen peroxide twice a day for seven days. Tooth color was evaluated before, 3 and 7 days of treatment, and 14 days after bleaching using a tooth color shade guide (VITA® shade). Tooth sensitivity was assessed using the Visual Analogue Scale (VAS). The values obtained from the color changes and tooth sensitivity were statistically analyzed (α=5%). RESULTS: For both groups, there was a significant difference on the tooth color before and after bleaching (P<0.001), although there was no significant difference between them (P=0.4215). The SB group exhibited a lower frequency of sensitivity (50.2%) compared to the TB group (70.2%) (P<0.001). However, the highest number of individuals reporting score 1 of sensitivity was found in the SB group (37.3%) compared to the TB group (20.9%) (P<0.001). For the other scores, there were no differences between the SB and TB groups, with results of 9.8% and 8.4% for score 2 (P=0.744) and 2.7% and 0.5% for score 3 (P=0.122). CONCLUSIONS: The bleaching effect of 10% hydrogen peroxide is not influenced by the delivering system (tray or strips). Even though the technique with strips was associated to a lower frequency of dental sensitivity, the peak level of pain was greater when compared to the technique using trays.

"Aerogels of enzymatically oxidized galactomannans from leguminous plants: Versatile delivery systems of antimicrobial peptides and enzymes".

We describe aerogels obtained by laccase/TEMPO-oxidation and lyophilization of galactomannans (GM) from fenugreek, sesbania and guar. Enzymatic oxidation of GM in aqueous solution caused viscosity increase up to fifteen-fold, generating structured, elastic, stable hydrogels, presumably due to establishment of hemiacetalic bonds between newly formed carbonyl groups and free hydroxyl groups. Upon lyophilization, water-insoluble aerogels were obtained, whose mechanical properties and porosity were investigated. Active principles were absorbed into the aerogels from aqueous solutions and, following rinsing, blotting, re-lyophilization, were released in an appropriate medium. The release of the antibiotic polymyxin B was tested against six different Gram-negative bacterial strains, of the antimicrobial peptide nisin against two Gram-positive and of the muraminidase lysozyme against one anaerobic strain. Protease and lipase release in solution from "enzyme loaded" aerogels was monitored by the increase in enzymatic activity. These biomaterials could represent new versatile, biocompatible "delivery systems" of actives for biomedical and industrial applications.

An aerogel obtained from chemo-enzymatically oxidized fenugreek galactomannans as a versatile delivery system.

We describe a new aerogel obtained from laccase-oxidized galactomannans of the leguminous plant fenugreek (Trigonella foenum-graecum) and suggest its potential practical use. Laccase/TEMPO oxidation of fenugreek in aqueous solution caused a viscosity increase of over 15-fold. A structured, elastic, stable hydrogel was generated, due to formation of carbonyl groups from primary OH of galactose side units and subsequent establishment of hemiacetalic bonds with available free hydroxyl groups. Upon lyophilization of this hydrogel, a water-insoluble aerogel was obtained (EOLFG), capable of uptaking aqueous or organic solvents over 20 times its own weight. The material was characterized by scanning electron microscopy, FT-IR, elemental analysis and (13)C CP-MAS NMR spectroscopy and its mechanical properties were investigated. To test the EOLFG as a delivery system, the anti-microbial enzyme lysozyme was used as model active principle. Lysozyme was added before or after formation of the aerogel, entrapped or absorbed in the gel, retained and released in active form, as proven by its hydrolytic glycosidase activity on lyophilized Micrococcus lysodeikticus cells wall peptidoglycans. This new biomaterial, composed of a chemo-enzymatically modified plant polysaccharide, might represent a versatile, biocompatible "delivery system" of active principles in food and non-food products.

Surface-Functionalization of Nanostructured Cellulose Aerogels by Solid State Eumelanin Coating.

Bioinspired aerogel functionalization by surface modification and coating is in high demand for biomedical and technological applications. In this paper, we report an expedient three-step entry to all-natural surface-functionalized nanostructured aerogels based on (a) TEMPO/NaClO promoted synthesis of cellulose nanofibers (TOCNF); (b) freeze-drying for aerogel preparation; and (c) surface coating with a eumelanin thin film by ammonia-induced solid state polymerization (AISSP) of 5,6-dihydroxyindole (DHI) or 5,6-dihydroxyindole-2-carboxylic acid (DHICA) previously deposited from an organic solution. Scanning electron microscopy showed uniform deposition of the dark eumelanin coating on the template surface without affecting porosity, whereas solid state (13)C NMR and electron paramagnetic resonance (EPR) spectroscopy confirmed the eumelanin-type character of the coatings. DHI melanin coating was found to confer to TOCNF templates a potent antioxidant activity, as tested by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) assays as well as strong dye adsorption capacity, as tested on methylene blue. The unprecedented combination of nanostructured cellulose and eumelanin thin films disclosed herein implements an original all-natural multifunctional aerogel biomaterial realized via an innovative coating methodology.

Multicomponent versus domino reactions: One-pot free-radical synthesis of ß-amino-ethers and ß-amino-alcohols.

Following an optimized multicomponent procedure, an aryl amine, a ketone, and a cyclic ether or an alcohol molecule are assembled in a one-pot synthesis by nucleophilic radical addition of ketyl radicals to ketimines generated in situ. The reaction occurs under mild conditions by mediation of the TiCl4/Zn/t-BuOOH system, leading to the formation of quaternary ß-amino-ethers and -alcohols. The new reaction conditions guarantee good selectivity by preventing the formation of secondary products. The secondary products are possibly derived from a competitive domino reaction, which involves further oxidation of the ketyl radicals.

TEMPO-Oxidized Cellulose Cross-Linked with Branched Polyethyleneimine: Nanostructured Adsorbent Sponges for Water Remediation.

Adsorbent sponges for water remediation were prepared using TEMPO-oxidized cellulose nanofibers (TOCNFs) as three-dimensional scaffolds, and branched polyethyleneimine (bPEI, 25 KDa) as the cross-linking agent. TOCNFs were suspended in aqueous solution in the presence of variable amounts of bPEI. The mixtures were first freeze-dried and then thermally treated (from 60 to 102 °C over 10 h) promoting the formation of amide bonds between the carboxylic groups of TOCNF and the primary amines of bPEI. The resulting materials, which were characterized by FTIR and 13 C CP-MAS NMR spectroscopy, scanning electron microscopy, and elemental analysis, showed higher chemical and mechanical stability in water than non-reticulated cellulose composites. The high adsorption capability of the new sponges was verified for different organic pollutants (p-nitrophenol, 2,4,5-trichlorophenol, and amoxicillin), and heavy metal ion pollutants (Cu, Co, Ni, Cd), indicating their potential for water decontamination.

Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.

A peculiar feature of the psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis (PhSOD) is the presence in its amino acid sequence of a reactive cysteine (Cys57). To define the role of this residue, a structural characterization of the effect of two PhSOD mutations, C57S and C57R, was performed. Thermal and denaturant-induced unfolding of wild type and mutant PhSOD followed by circular dichroism and fluorescence studies revealed that C→R substitution alters the thermal stability and the resistance against denaturants of the enzyme, whereas C57S only alters the stability of the protein against urea. The crystallographic data on the C57R mutation suggest an involvement of the Arg side chain in the formation of salt bridges on protein surface. These findings support the hypothesis that the thermal resistance of PhSOD relies on optimization of charge-charge interactions on its surface. Our study contributes to a deeper understanding of the denaturation mechanism of superoxide dismutases, suggesting the presence of a structural dimeric intermediate between the native state and the unfolded state. This hypothesis is supported by the crystalline and solution data on the reduced form of the enzyme.

New advances in titanium-mediated free radical reactions.

Titanium complexes have been widely used as catalysts for C­C bond-forming processes via free-radical routes. Herein we provide an overview of some of the most significant contributions in the field, that covers the last decade, emphasizing the key role played by titanium salts in the promotion of selective reactions aimed at the synthesis of multifunctional organic compounds, including nucleophilic radical additions to imines, pinacol and coupling reactions, ring opening of epoxides and living polymerization.

Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans.

Superoxide dismutases are enzymes that protect biological systems against oxidative damage caused by superoxide radicals. In this paper, a detailed characterization is presented on the stability of SmSOD, the dimeric cambialistic superoxide dismutase from the dental pathogenic microorganism Streptococcus mutans, towards temperature and guanidine hydrochloride. Thermal and chemical denaturations were investigated by means of circular dichroism, fourth-derivative UV spectroscopy and fluorescence measurements. Data indicate that SmSOD is endowed with a significant thermostability and that both its thermal and guanidine hydrochloride-induced unfolding processes occur through a three-state model, characterized by a catalytically active dimeric intermediate species. To our knowledge, SmSOD is the smallest known dimeric protein that populates a well-structured active dimeric rather than a monomeric intermediate during unfolding processes.

Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.

Superoxide dismutases (SODs) are metalloenzymes catalysing the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Here, we present the crystal structure of a cold-adapted Fe-SOD from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhSOD), and that of its complex with sodium azide. The structures were compared with those of the corresponding homologues having a high sequence identity with PhSOD, such as the mesophilic SOD from Escherichia coli (EcSOD) or Pseudomonas ovalis, and the psychrophilic SOD from Aliivibrio salmonicida (AsSOD). These enzymes shared a large structural similarity, such as a conserved tertiary structure and arrangement of the two monomers, an almost identical total number of inter- and intramolecular hydrogen bonds and salt bridges. However, the two cold-adapted SODs showed an increased flexibility of the active site residues with respect to their mesophilic homologues. Structural information was combined with a characterisation of the chemical and thermal stability performed by CD and fluorescence measurements. Despite of its psychrophilic origin, the denaturation temperature of PhSOD was comparable with that of the mesophilic EcSOD, whereas AsSOD showed a lower denaturation temperature. On the contrary, the values of the denaturant concentration at the transition midpoint were in line with the psychrophilic/mesophilic origin of the proteins. These data provide additional support to the hypothesis that cold-adapted enzymes achieve efficient catalysis at low temperature, by increasing the flexibility of their active site; moreover, our results underline how fine structural modifications can alter enzyme flexibility and/or stability without compromising the overall structure of typical rigid enzymes, such as SODs.