scholarly journals Quantitative analysis of Protective Role of salivary protein on demineralization of enamel

2021 ◽  
Vol 15 (8) ◽  
pp. 2457-2459
Author(s):  
Asadullah Rathore ◽  
Anwar Alam ◽  
Marryam Riaz ◽  
Asma Arshad ◽  
Maria Javed ◽  
...  
Keyword(s):  
Spot Size ◽  
Protective Role ◽  
Salivary Protein ◽  
Sem Analysis ◽  
Salivary Proteins ◽  
Protein Solutions ◽  
Contour Maps ◽  
Prismatic Structure ◽  
Demineralized Enamel ◽  
Diffraction Patterns

Objective: The aim of this study was to analyze the effect of salivary proteins (statherin and histatin-1) on demineralized enamel surface and to study changes in texture, magnitude and direction of crystallites and changes in prismatic structure of enamel respectively. Material & Methods: Synchrotron x-ray diffraction technique to determine the variation in degree of crystal orientation (texture). Incisors were demineralized and sectioned to 300-500 microns, rinsed with salivary protein solutions of statherin and histatin separately and in combination with short and full-lengths. A beam spot size of 20μm × 20μm was used to obtain 2D diffraction patterns to distinguish orientation of crystallites. Results: The contour maps as well as the SEM analysis present similar surface properties of the sample treated with STN-21 and the controlled PBS sample. Therefore, STN-21 was found potent in preventing demineralization and restoring surface enamel texture followed by STN-21+HTN-21 and STN43+HTN38. HTN-21 and HTN-38 showed similar demineralization pattern as the controlled demineralized sample. Conclusion: Ranking of demineralization among samples was found to be controlled demineralized > HTN-21 = HTN-38 > STN-43+HTN-38 > STN-21+HTN-21 > STN-21. Developing STN-21 as a therapeutic against dental caries and erosion. Keywords: Enamel, Demineralization, salivary proteins.

Immediate Erosive Potential of Cola Drinks and Orange Juices

2006 ◽  
Vol 85 (3) ◽  
pp. 226-230 ◽  
Author(s):  
T. Jensdottir ◽  
P. Holbrook ◽  
B. Nauntofte ◽  
C. Buchwald ◽  
A. Bardow
Keyword(s):  
Soft Drink ◽  
Titratable Acidity ◽  
Protective Role ◽  
Salivary Protein ◽  
Soft Drinks ◽  
Salivary Proteins ◽  
Hydroxyapatite Crystals

Little is known about the erosive potential of soft drinks within the first minutes of exposure to teeth, and about the potentially protective role of salivary proteins. We hypothesized that the erosive potential is determined primarily by pH and decreases in the presence of salivary proteins. To investigate this, we first added uncoated hydroxyapatite crystals and, second, salivary-protein-coated hydroxyapatite crystals to 20 commercially available cola drinks and orange juices simultaneously, with pH recordings every 15 sec for 3 min. The amount of apatite lost per liter of soft drink per sec was calculated from titratable acidity values to each pH obtained by crystal addition. The erosive potential within the first minutes of exposure was determined solely by the pH of the drink, and the erosive potential was ten-fold higher in cola drinks compared with juices. However, salivary proteins reduced the erosive potential of cola drinks by up to 50%.

scholarly journals A Comparative Evaluation of Nanohydroxyapatite-Enriched Hydrogen Peroxide Home Bleaching System on Color, Hardness and Microstructure of Dental Enamel

Materials ◽  
2021 ◽  
Vol 14 (11) ◽  
pp. 3072
Author(s):  
Riccardo Monterubbianesi ◽  
Vincenzo Tosco ◽  
Tiziano Bellezze ◽  
Giampaolo Giuliani ◽  
Mutlu Özcan ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Particle Diameter ◽  
Dental Enamel ◽  
Sem Analysis ◽  
Control Group ◽  
Average Particle ◽  
Color Analysis ◽  
Enamel Microstructure ◽  
Prismatic Structure ◽  
20 Nm

This study aimed to evaluate two hydrogen peroxide (HP)-based at-home bleaching systems in order to analyze whether nano-hydroxyapatite (nHA) addition may represent a reliable and safe solution for tooth whitening without altering dental microstructure and hardness. Human third molars (N = 15) were treated with two bleaching agents, one containing 6%HP (6HP) and the other 6% HP nHA-enriched (6HP-nHA) with average particle diameter ranging from 5–20 nm. Their effects on enamel were assessed using a spectrophotometer, Vickers microhardness (VMH) test and Scanning Electron Microscopy (SEM), comparing the treated groups with the non-treated control group (CTR). Color analysis revealed improvement in whiteness in both groups compared to CTR. VMH test results showed no differences among the groups. SEM analysis highlighted no evident changes in the enamel microstructure of tested groups compared to CTR. At high magnification, in 6HP group, a slight increase in irregularities of enamel surface morphology was observed, while 6HP-nHA group displayed removal of the aprismatic layer but preservation of the intact prismatic structure. These results suggest that the 6HP-nHA agent may be recommended to provide reliable whitening treatment, without damaging the enamel micromorphology and hardness.

The crystallography of calf rennin (chymosin)

1971 ◽  
Vol 178 (1052) ◽  
pp. 245-258 ◽  
Keyword(s):  
Degradation Products ◽  
Protein Solutions ◽  
Stable Range ◽  
X Ray Diffraction ◽  
Stable Species ◽  
Wide Range ◽  
Unit Cells ◽  
Diffraction Patterns ◽  
The Stability ◽  
Ph Range

The growth of crystals of calf rennin (chymosin, † EC 3.4.4.3) and the control of nucleation to produce crystals of desired size, are described. Only one stable species, orthorhombic rennin I, has been found, but a metastable monoclinic species, rennin II, appeared on one occasion in a solution nearly saturated with glycine. The morphology, optical characteristics and unit cells of these species are recorded. In rennin I, small differences in the properties of sectors built by deposition on the three types of crystal faces are attributed to differences in the proportions of either degradation products or of the slightly different isoenzymes known to be present in calf rennin. Rennin I crystals have been obtained only within the pH range of greatest stability of the protein, 5. 0 to 6. 2; but the crystals tolerate subsequent changes of pH down to 2. 0. The stability of crystals appears to be much greater than that of salt-free protein solutions. Rennin I may be crosslinked with glutaraldehyde with no loss of order, giving crystals stable over a wide range of solution conditions, including pH 2.0 to 10.0 and salt-free solutions. The remarkable swelling behaviour when the pH is raised beyond the stable range is described. Rennin II, though monoclinic in symmetry, shows in its X -ray diffraction patterns strong evidence of a pseudo-orthorhombic arrangement of molecules.

Salivary Proteins Interact with Dietary Constituents to Modulate Tooth Staining

2005 ◽  
Vol 84 (1) ◽  
pp. 73-78 ◽  
Author(s):  
G.B. Proctor ◽  
R. Pramanik ◽  
G.H. Carpenter ◽  
G.D. Rees
Keyword(s):  
Red Wine ◽  
Black Tea ◽  
Salivary Protein ◽  
Salivary Proteins ◽  
Parotid Saliva ◽  
Grape Skin ◽  
Dietary Components ◽  
Black Tea Polyphenols ◽  
Proline Rich Protein

Dietary components rich in polyphenols—for example, tea and red wine—are thought to cause tooth staining. In the present study, hydroxyapatite was used as a model of enamel for study of the influence of salivary proteins on the binding of different polyphenols to hydroxyapatite in vitro. Neither salivary protein pellicles nor salivary proteins in solution significantly altered the binding of the small polyphenol epigallocatechin to hydroxyapatite. However, hydroxyapatite binding of anthocyanin, a small grape-skin-derived polyphenol, or the larger polyphenols of black tea was increased by the presence of salivary proteins, either as a pellicle or in solution. Proline-rich proteins were enriched from parotid saliva and found to increase binding of anthocyanin and black tea polyphenols to hydroxyapatite, while enriched histatins did not increase binding. It is concluded that some salivary proteins, including proline-rich protein, can mediate increased staining of enamel by red-wine- and black-tea-derived polyphenols.

scholarly journals Host Defense Proteins Derived from Human Saliva Bind to Staphylococcus aureus

2013 ◽  
Vol 81 (4) ◽  
pp. 1364-1373 ◽  
Author(s):  
Seok-Mo Heo ◽  
Kyoung-Soo Choi ◽  
Latif A. Kazim ◽  
Molakala S. Reddy ◽  
Elaine M. Haase ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Oral Cavity ◽  
Host Defense ◽  
Bacterial Colonization ◽  
Human Saliva ◽  
Salivary Protein ◽  
Salivary Proteins ◽  
Staphylococcal Protein A ◽  
Defense Proteins ◽  
Content Type

ABSTRACTProteins in human saliva are thought to modulate bacterial colonization of the oral cavity. Yet, information is sparse on how salivary proteins interact with systemic pathogens that transiently or permanently colonize the oral environment.Staphylococcus aureusis a pathogen that frequently colonizes the oral cavity and can cause respiratory disease in hospitalized patients at risk. Here, we investigated salivary protein binding to this organism upon exposure to saliva as a first step toward understanding the mechanism by which the organism can colonize the oral cavity of vulnerable patients. By using fluorescently labeled saliva and proteomic techniques, we demonstrated selective binding of major salivary components byS. aureusto include DMBT1gp-340, mucin-7, secretory component, immunoglobulin A, immunoglobulin G, S100-A9, and lysozyme C. Biofilm-grownS. aureusstrains bound fewer salivary components than in the planctonic state, particularly less salivary immunoglobulins. A corresponding adhesive component on theS. aureussurface responsible for binding salivary immunoglobulins was identified as staphylococcal protein A (SpA). However, SpA did not mediate binding of nonimmunoglobulin components, including mucin-7, indicating the involvement of additional bacterial surface adhesive components. These findings demonstrate that a limited number of salivary proteins, many of which are associated with various aspects of host defense, selectively bind toS. aureusand lead us to propose a possible role of saliva in colonization of the human mouth by this pathogen.

scholarly journals In Vitro Salivary Protein Adsorption Profile on Titanium and Ceramic Surfaces and the Corresponding Putative Immunological Implications

2020 ◽  
Vol 21 (9) ◽  
pp. 3083 ◽  
Author(s):  
Chen-Xuan Wei ◽  
Michael Francis Burrow ◽  
Michael George Botelho ◽  
Henry Lam ◽  
Wai Keung Leung
Keyword(s):  
Immune Responses ◽  
Interaction Network ◽  
Salivary Protein ◽  
Microbial Interactions ◽  
Salivary Proteins ◽  
Material Surface ◽  
Go Annotation ◽  
Implant Abutment ◽  
Adsorbed Proteins

Immune responses triggered by implant abutment surfaces contributed by surface-adsorbed proteins are critical in clinical implant integration. How material surface-adsorbed proteins relate to host immune responses remain unclear. This study aimed to profile and address the immunological roles of surface-adsorbed salivary proteins on conventional implant abutment materials. Standardized polished bocks (5 × 5 × 1 mm3) were prepared from titanium and feldspathic ceramic. Salivary acquired pellicle formed in vitro was examined by liquid chromatography-tandem mass spectrometry and gene ontology (GO) analysis to identify and characterize the adsorbed proteins. Out of 759 proteins identified from pooled saliva samples, 396 were found to be attached to the two materials tested—369 on titanium and 298 on ceramic, with 281 common to both. GO annotation of immune processes was undertaken to form a protein–protein interaction network, and 14 hub proteins (≥6 interaction partners) (coding genes: B2M, C3, CLU, DEFA1, HSP90AA1, HSP90AB1, LTF, PIGR, PSMA2, RAC1, RAP1A, S100A8, S100A9, and SLP1) were identified as the key proteins connecting multiple (6–9) immune processes. The results offered putative immunological prospects of implant abutment material surface-adsorbed salivary proteins, which could potentially underpin the dynamic nature of implant–mucosal/implant–microbial interactions.

Molecular Cloning of Developmentally Regulated Neonatal Rat Submandibular Gland Proteins

1993 ◽  
Vol 4 (3) ◽  
pp. 525-530 ◽  
Author(s):  
Lily Mirels ◽  
Lisa R. Girard ◽  
William D. Ball
Keyword(s):  
Molecular Cloning ◽  
Submandibular Gland ◽  
Cdna Library ◽  
Protein C ◽  
Salivary Protein ◽  
Neonatal Rat ◽  
Salivary Proteins ◽  
Developmentally Regulated ◽  
Rat Submandibular Gland

At birth, the rat submandibular gland (SMG) contains two transient secretory cell types that produce several characteristic salivary proteins. Proteins SMG-A, B1, and B2 (23.5, 26 and 27.5 kDa) are products of the neonatal type III cells, but not the adult acinar cells. Protein C (89 kDa), a major product of the neonatal type I cells, is either absent or present at greatly diminished levels in the secretory cells of the adult gland. The decrease in biosynthesis of these neonatal salivary proteins occurs concomitantly with the increase in levels of characteristic adult SMG products. In order to understand these developmentally regulated changes in SMG salivary protein gene expression, we have initiated the molecular cloning and characterization of neonatal submandibular gland proteins from a 5-d-old rat submandibular gland cDNA library. Clones encoding SMG-A were isolated by homology to the mouse parotid secretory protein (PSP). SMG-A was shown to be derived from a salivary protein multigene family that also includes PSP. Cloning and characterization of additional neonatal rat submandibular gland proteins was initiated by screening the 5-d-old rat submandibular gland cDNA library with first strand cDNA prepared from 1-d-old rat submandibular glands. Clones corresponding to a highly abundant 3 kb transcript present in the neonatal rat SMG, but not in adult submandibular, sublingual, or parotid gland have been identified. The size, abundance, and organ specificity of this transcript suggest that it may encode protein C. One clone derived from an unknown transcript that is developmentally regulated in the neonatal SMG and is present in the adult parotid, submandibular, and sublingual glands was also identified.

scholarly journals Suppression of Plant Defenses by a Myzus persicae (Green Peach Aphid) Salivary Effector Protein

2014 ◽  
Vol 27 (7) ◽  
pp. 747-756 ◽  
Author(s):  
Dezi A. Elzinga ◽  
Martin De Vos ◽  
Georg Jander
Keyword(s):  
Myzus Persicae ◽  
Host Plants ◽  
Green Peach Aphid ◽  
Salivary Protein ◽  
Aphid Species ◽  
Salivary Proteins ◽  
Buchnera Aphidicola ◽  
Complex Interactions ◽  
Species Specific ◽  
Phloem Feeding

The complex interactions between aphids and their host plant are species-specific and involve multiple layers of recognition and defense. Aphid salivary proteins, which are released into the plant during phloem feeding, are a likely mediator of these interactions. In an approach to identify aphid effectors that facilitate feeding from host plants, eleven Myzus persicae (green peach aphid) salivary proteins and the GroEL protein of Buchnera aphidicola, a bacterial endosymbiont of this aphid species, were expressed transiently in Nicotiana tabacum (tobacco). Whereas two salivary proteins increased aphid reproduction, expression of three other aphid proteins and GroEL significantly decreased aphid reproduction on N. tabacum. These effects were recapitulated in stable transgenic Arabidopsis thaliana plants. Further experiments with A. thaliana expressing Mp55, a salivary protein that increased aphid reproduction, showed lower accumulation of 4-methoxyindol-3-ylmethylglucosinolate, callose and hydrogen peroxide in response to aphid feeding. Mp55-expressing plants also were more attractive for aphids in choice assays. Silencing Mp55 gene expression in M. persicae using RNA interference approaches reduced aphid reproduction on N. tabacum, A. thaliana, and N. benthamiana. Together, these results demonstrate a role for Mp55, a protein with as-yet-unknown molecular function, in the interaction of M. persicae with its host plants.

scholarly journals Green Synthesis, Texture, Electron Diffraction, Thermal and Optical Properties of Cobalt Doped Arginine Carbon Nanotubes

2021 ◽  
Vol 33 (5) ◽  
pp. 1120-1124
Author(s):  
Sarvesh Kumar Shailesh ◽  
B. Tiwari ◽  
K. Yadav
Keyword(s):  
Carbon Nanotubes ◽  
Electron Diffraction ◽  
Green Synthesis ◽  
Chemical Precipitation ◽  
Sem Analysis ◽  
Precipitation Method ◽  
Tem Analysis ◽  
Force Microscopy ◽  
Diffraction Patterns ◽  
20 Nm

In this work, a simple and viable method of green synthesis of multi-walled cobalt doped arginine carbon nanotubes (CNT’s) by chemical precipitation method using arginine amino acid is reported. The atomic force microscopy confirmed that metal ions present in a branched fashion on the surface of Co-doped arginine CNT’s and the obtained particle with diameter 20 nm well dispersed on the carbon nanotubes. The TEM analysis indicates the interlayer separation between the two adjacent carbon walls is estimated to be about 0.34 nm. The electron diffraction patterns indicate that the tube has nearly identical chirality for all of the concentric graphitic layers, as a zigzag-type MWCNT. The SEM analysis predicted tube like morphology and strain is existed on the surface of the CNTs. The Raman spectra confirmed the armchair (n = 8 to 11) multi-walled nanotubes with this chirality are assigned as a semiconducting type of nanotubes. The thermal property was studied by thermogravimetric analysis, differential thermal analysis and predicted the 27.81 % purity in CNTs.

scholarly journals Physicochemical Research of Clinically Retrieved CU-NI-TI Orthodontic Archwires

2021 ◽  
Vol 48 (1) ◽  
pp. 68-74
Author(s):  
A. Stoyanova-Ivanova ◽  
V. Petrov ◽  
V. Petrova ◽  
L. Andreeva ◽  
I. Ilievska ◽  
...  
Keyword(s):  
Chemical Composition ◽  
Structural Changes ◽  
Rectangular Cross Section ◽  
Sem Analysis ◽  
Scanning Calorimetry ◽  
Chemical Content ◽  
Diffraction Patterns ◽  
Xrd Patterns ◽  
Orthodontic Archwires ◽  
Bio Compatibility

Abstract In modern orthodontics, thermally activated archwires are used more widely in clinical practice, because they have unique properties like superelasticity and bio-compatibility. The aim of the present study was to characterize commercial 35° C Cu-NiTi archwires in terms of their phase transition behavior, chemical composition, surface topography properties after clinical usage, as well as the influence of the autoclaving process. Materials and methods. 35° C Thermo-Active Copper NiTi (CuNiTi) of ORMCO, Glendora, CA, USA (as-received, as-received autoclaved and clinically retrieved) with rectangular cross-section and dimension 0.016x0.022 inch, were investigated. The physicochemical research was conducted via Differential Scanning Calorimetry (DSC), Scanning Electron Microscopy (SEM), Energy Dispersive Spectroscopy (EDX) and X-ray Diffraction Analysis (XRD). The autoclaving was done in Runyes model B autoclave. Results. The DSC results revealed the austenite start (9.8° C; 26.47° C) and austenite finish (28° C; 31.74° C) temperatures for the as-received and autoclaved archwires respectively. For clinically retrieved samples the austenite finish temperature (Af) is around 27° C. The XRD patterns of the as-received and clinically retrieved samples show almost identical diffraction patterns. Rough surface of the CuNiTi alloy was revealed by the SEM analysis. Autoclaving process seems to have no effects on archwires’ structure and chemical composition. Chemical content of the investigated as-received CuNiTi are Ni, Ti and Cu: 47.07 wt% and 46.81 wt% and 6.11 wt%, respectively. The autoclaving process seems to have little influence on the transition temperature. The results from our study showed little difference (~7 °C) in the finish transition temperatures (Af), compared to the manufacturer’s claim. No intermediate R phase was detected by DSC. Conclusion. A good knowledge of the structural changes that occur in CuNiTi alloys in the oral cavity is useful for the orthodontists in order to optimize orthodontic treatment.

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