Early Bone Healing and Biomechanical Fixation of Dual Acid-Etched and As-Machined Implants with Healing Chambers: An Experimental Study in Dogs

Purpose: To evaluate the biomechanical fixation, bone-to-implant contact (BIC), and bone morphology of screw-type root-form implants with healing chambers with as-machined or dual acid-etched (DAE) surfaces in a canine model. Materials and Methods: The animal model included the placement of machined (n = 24) and DAE (n = 24) implants along the proximal tibiae of six mongrel dogs, which remained in place for 2 or 4 weeks. Following euthanasia, half of the specimens were subjected to biomechanical testing (torque to interface failure) and the other half were processed for histomorphologic and histomorphometric (%BIC) assessments. Statistical analyses were performed by one-way analysis of variance at the 95% confidence level and the Tukey post hoc test for multiple comparisons. Results: At 4 weeks, the DAE surface presented significantly higher mean values for torque to interface failure overall. A significant increase in %BIC values occurred for both groups over time. For both groups, bone formation through the classic appositional healing pathway was observed in regions where intimate contact between the implant and the osteotomy walls occurred immediately after implantation. Where contact-free spaces existed after implantation (healing chambers), an intramembranous-like healing mode with newly formed woven bone prevailed. Conclusions: In the present short-term evaluation, no differences were observed in BIC between groups; however, an increase in biomechanical fixation was seen from 2 to 4 weeks with the DAE surface. INT J ORAL MAXILLOFAC IMPLANTS 2011;26:75-82

Biomechanical and histologic evaluation of non-washed resorbable blasting media and alumina-blasted/acid-etched surfaces

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Influence of root-surface conditioning with acid and chelating agents on clot stabilization

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Response of human pulps following acid conditioning and application of a bonding agent in deep cavities

Objectives. The aim of this in vivo study was to evaluate the human dental pulp response when a one-bottle adhesive system was applied on etched or unetched deep dentine.Methods. Eighteen class V deep cavity preparations were divided in three groups: group 1-total etching + two coats of single bond (SB) + composite resin (Z-100); group 2-enamel etching + two coats of SB + Z-100, group 3-cavity floor lined with a calcium hydroxide liner (Dycal) + acid-etching of enamel and lateral walls + two coats of SB + Z-100. Two teeth were used as intact control group. After 30 days the teeth were extracted and processed through H and E, Masson's trichrome and Brown and Brenn staining techniques.Results. Moderate inflammatory response, disorganization of pulp tissue, as well as, deposition of thin layer of reactionary dentin were observed in group 1 teeth in which the remaining dentin thickness (RDT) was less than 300 mum. These histological findings appear to be related to long resin tags formation and bonding agent diffusion through dentinal tubules. In group 2, slight inflammatory response was observed only in one tooth in which the RDT was 162 mum. In group 3, all the teeth showed normal histological characteristics which were similar to the intact control group. Presence of bacteria was not correlated with the intensity of pulpal response. The patients reported no symptoms during the experiment. Radiographic evaluation showed no periapical pathology for any of the teeth,Significance and conclusions. Acid-etched deep dentin (RDT less than 300 mum) lined with SB causes more intense pulpal response than unetched deep dentin. Based on the results observed in the present study and the conditions in which it was carried out, we recommend the application of a biocompatible liner before etching deep dentin and applying SB. (C) 2002 Academy of Dental Materials. Published by Elsevier B.V. Ltd. All rights reserved.

Effect of acid etching time on the degradation of resin-dentin bonds in primary teeth

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Penetration into dentin of sodium hypochlorite associated with acid solutions

Objective. The objective of this study was to evaluate the penetration of 2.5% NaOCl associated with 17.0% EDTA, 1.0% citric acid, and 1.0% peracetic acid into dentin tubules.Study design. The roots of 44 bovine incisors were cross-sectioned and 5-mm-long fragments were produced from their middle thirds. The specimens were instrumented with ProTaper hand files, stained in crystal violet, then sectioned mesiodistally. The buccal fragments were divided into 4 groups (n = 9) and subjected to 2 consecutive 10-minute immersion periods in one of the following acid solutions combined with 2.5% NaOCl: 17.0% EDTA (group 1), 1.0% citric acid (group 2), and 1.0% peracetic acid (group 3). Nine fragments were immersed in 2.5% NaOCl (group 4). The analysis of the penetration of NaOCl solutions into dentin was performed by measuring the depth of crystal violet stain that was bleached using a steromicroscope under x50 magnification. Statistical comparisons were carried out by Kruskal-Wallis and Dunn's tests at the 5% significance level.Results. Group 1 showed less penetration into dentin than group 4 (P < .05). No statistically significant differences were observed among groups 2, 3, and 4 (P > .05).Conclusions. Association of NaOCl with acid solutions did not increase its penetration depth into root dentin. (Oral Surg Oral Med Oral Pathol Oral Radiol Endod 2011;112:e155-e159)

Structural insights for fatty acid binding in a Lys49-phospholipase A(2): crystal structure of myotoxin II from Bothrops molojeni complexed with stearic acid

The crystal structure of dimeric Lys49-phospholipase A2 myotoxin-II from Bothrops moojeni (MjTX-II) co-crystallized with stearic acid (C18H36O2) has been determined at a resolution of 1.8 angstrom. The electron density maps permitted the unambiguous inclusion of six stearic acid molecules in the refinement. Two stearic acid molecules could be located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of legend-protein complex. The comparison of MjTX-II/satiric acid complex with other Lys-PLA(2)s structures whose putative fatty acids were located at their active site is also analysed. Molecular details of the stearic acid/protein interactions provide insights to binding in croup I/II PLA(2)s and to the possible interactions of Lys49-PLA(2)s with target membranes. (c) 2004 Elsevier SAS. All rights reserved.

Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A(2) homologue from Bothrops pirajai venom complexed with rosmarinic acid

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Messenger ribonucleic acid abundance of intestinal enzymes and transporters in feed-restricted and refed chickens at different ages

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

SOLID STATE ELECTROCHEMICAL BEHAVIOR of USNIC ACID AT A GLASSY CARBON ELECTRODE

The electrochemical redox behavior of usnic acid, mainly known for its antibiotic activity, has been investigated using cyclic, differential pulse and square wave voltammetry in aqueous electrolyte. These studies were carried out by solid state voltammetry with the solid mechanically attached on the surface of a glassy carbon electrode and at different pH values. Usnic acid did not present any reduction reaction. The pH-dependent electrochemical oxidation occurs in three steps, one electron and one proton irreversible processes, assigned to each of the hydroxyl groups in the molecule. Adsorption of the non-electroactive oxidation product was also observed, blocking the electrode surface. An oxidation mechanism was proposed and electroanalytical methodology was developed to determine usnic acid.

Interaction of shikimic acid with shikimate kinase (Retracted Article. See vol 334, pg 967, 2005)

The crystal structure of shikimate kinase from Mycobacterium tuberculosis (MtSK) complexed with MgADP and shikimic acid (shikimate) has been determined at 2.3 Angstrom resolution, clearly revealing the amino acid residues involved in shikimate binding. In MtSK, the Glu61 strictly conserved in SK forms a hydrogen bond and salt-bridge with Arg58 and assists in positioning the guanidinium group of Arg58 for shikimate binding. The carboxyl group of shikimate interacts with Arg58, Gly81, and Arg136, and hydroxyl groups with Asp34 and Gly80. The crystal structure of MtSK-MgADP-shikimate will provide crucial information for elucidation of the mechanism of SK-catalyzed reaction and for the development of a new generation of drugs against tuberculosis. (C) 2004 Elsevier B.V. All rights reserved.

Structure of shikimate kinase from Mycobacterium tuberculosis reveals the binding of shikimic acid

Tuberculosis made a resurgence in the mid-1980s and now kills approximately 3 million people a year. The re-emergence of tuberculosis as a public health threat, the high susceptibility of HIV-infected persons and the proliferation of multi-drug-resistant strains have created a need to develop new drugs. Shikimate kinase and other enzymes in the shikimate pathway are attractive targets for development of non-toxic antimicrobial agents, herbicides and anti-parasitic drugs, because the pathway is essential in these species whereas it is absent from mammals. The crystal structure of shikimate kinase from Mycobacterium tuberculosis (MtSK) complexed with MgADP and shikimic acid ( shikimate) has been determined at 2.3 Angstrom resolution, clearly revealing the amino-acid residues involved in shikimate binding. This is the first three-dimensional structure of shikimate kinase complexed with shikimate. In MtSK, the Glu61 residue that is strictly conserved in shikimate kinases forms a hydrogen bond and salt bridge with Arg58 and assists in positioning the guanidinium group of Arg58 for shikimate binding. The carboxyl group of shikimate interacts with Arg58, Gly81 and Arg136 and the hydroxyl groups interact with Asp34 and Gly80. The crystal structure of MtSK-MgADP-shikimate will provide crucial information for the elucidation of the mechanism of the shikimate kinase-catalyzed reaction and for the development of a new generation of drugs against tuberculosis.

Ultrastructural changes in the ovary cells of engorged Rhipicephalus sanguineus female ticks treated with esters of ricinoleic acid from castor oil (Ricinus communis)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Morphological alterations induced by boric acid and fipronil in the midgut of worker honeybee (Apis mellifera L.) larvae

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities

BaP1 is a 22.7-kD P-I-type zinc-dependent metalloproteinase isolated from the venom of the snake Bothrops asper, a medically relevant species in Central America. This enzyme exerts multiple tissue-damaging activities, including hemorrhage, myonecrosis, dermonecrosis, blistering, and edema. BaP1 is a single chain of 202 amino acids that shows highest sequence identity with metalloproteinases isolated front the venoms of snakes of the subfamily Crotalinae. It has six Cys residues involved in three disulfide bridges (Cys 117-Cys 197, Cys 159-Cys 181, Cys 157-Cys 164). It has the consensus sequence H(142)E(143)XXH(146)XXGXXH(152), as well as the sequence C164I165M166, which characterize the metzincin superfamily of metalloproteinases. The active-site cleft separates a major subdomain (residues 1-152), comprising four a-helices and a five-stranded beta-sheet, from the minor subdomain, which is formed by a single a-helix and several loops. The catalytic zinc ion is coordinated by the N-epsilon2 nitrogen atoms of His 142, His 146, and His 152, in addition to a solvent water molecule, which in turn is bound to Glu 143. Several conserved residues contribute to the formation of the hydrophobic pocket, and Met 166 serves as a hydrophobic base for the active-site groups. Sequence and structural comparisons of hemorrhagic and nonhemorrhagic P-I metalloproteinases from snake venoms revealed differences in several regions. In particular, the loop comprising residues 153 to 176 has marked structural differences between metalloproteinases with very different hemorrhagic activities. Because this region lies in close proximity to the active-site microenvironment, it may influence the interaction of these enzymes with physiologically relevant substrates in the extracellular matrix.