Related Experiment Video
Updated: Jan 26, 2026
09:49
Routine Screening Method for Microparticles in Platelet Transfusions
Published on: January 31, 2018
16.5K
Effect of Methods of Biosilicate Microparticle Application on Dentin Adhesion
Michelle Alexandra Chinelatti1, Egle Leitão Santos2, Camila Tirapelli3
1Department of Dental Materials and Prosthodontics, Ribeirão Preto School of Dentistry, University of São Paulo, Av. do Café s/n, Monte Alegre, Ribeirão Preto, São Paulo 14040-904, Brazil. chinelatti@usp.br.
Dentistry Journal
|April 4, 2019
Summary
Biosilicate microparticle treatments enhance dentin bond strength for minimally invasive dentistry. Both blasting and paste methods improved adhesion compared to no treatment, without negatively impacting the adhesive interface.
Area of Science:
- Biomaterials Science
- Dental Materials Science
- Minimally Invasive Dentistry
Background:
- Bioglass restorative procedures align with minimally invasive dentistry principles.
- Evaluating biosilicate microparticle application methods is crucial for optimizing dental adhesion.
Purpose of the Study:
- To assess the bond strength of dentin treated with two distinct biosilicate microparticle application methods.
- To compare these treatments against a control group for restorative dental procedures.
Main Methods:
- Dentin surfaces of human molars were divided into three groups: biosilicate blasting, 10% biosilicate paste, and control.
- Restorations were performed using self-etch adhesive and nanofilled composite.
- Microtensile bond strength testing and scanning electron microscopy (SEM) analysis were conducted.
Main Results:
- Biosilicate-treated groups exhibited significantly higher bond strength than the control group (p < 0.05).
- No significant difference in bond strength was observed between the two biosilicate application methods (p > 0.05).
- SEM analysis confirmed proper hybridization and intact resin-dentin adhesive interfaces.
Conclusions:
- Biosilicate microparticle surface treatment positively influences dentin adhesion.
- Both evaluated biosilicate application methods are effective in enhancing bond strength.
- The treatments do not compromise the integrity of the adhesive interface, supporting their use in restorative dentistry.
Related Concept Videos
01:14Adhesion
43.7K
Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
Capillary action is a result of water’s adhesive tendencies. When a narrow...
Capillary action is a result of water’s adhesive tendencies. When a narrow...
43.7K
01:14Cell Adhesion in Plants
3.3K
Plants have rigid cell walls that are made up of cell wall polysaccharides that mediate cell-cell adhesion. The primary cell walls of plants consist of two independent and interacting polysaccharide networks: a pectin matrix that embeds the second network comprising cellulose and hemicelluloses.
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose,...
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose,...
3.3K
01:31Immunoglobulin-like Cell Adhesion Molecules
4.3K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.3K
01:17Intracellular Signaling Affects Focal Adhesions
3.5K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
3.5K
01:20Cell Adhesion Molecules - Types and Functions
9.2K
Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily involved...
CAM Families
The Integrin family of proteins is primarily involved...
9.2K
00:55Laminins are the Adhesive Proteins of Basal Lamina
3.1K
Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
3.1K