Proteins are found to be involved in interaction with solid surfaces in numerous natural events. Acidic proteins that adsorb to crystal faces of a biomineral to control the growth and morphology of hard tissue are only one example. Deducing the mechanisms of surface recognition exercised by proteins has implications to osteogenesis, pathological calcification and other proteins functions at their adsorbed state. Statherin is an enamel pellicle protein that inhibits hydroxyapatite nucleation and growth, lubricates the enamel surface, and is recognized by oral bacteria in periodontal diseases. Here, we highlight some of the insights we obtained recently using both thermodynamic and solid state NMR measurements to the adsorption process of statherin to hydroxyapatite. We combine macroscopic energy characterization with microscopic structural findings to present our views of protein adsorption mechanisms and the structural changes accompanying it and discuss the implications of these studies to understanding the functions of the protein adsorbed to the enamel surfaces.

Download full-text PDF

Source
http://dx.doi.org/10.1002/mrc.2123DOI Listing

Publication Analysis

Top Keywords

statherin hydroxyapatite
8
structure dynamics
4
dynamics energetics
4
protein
4
energetics protein
4
protein adsorption-lessons
4
adsorption-lessons learned
4
learned adsorption
4
adsorption statherin
4
proteins
4

Similar Publications

Article Synopsis
  • Energy-dispersive Laue diffraction (EDLD) is used to analyze the crystalline structure of dental enamel, focusing on how specific salivary peptides (statherin and histatin-1) affect demineralization processes.
  • Three groups of healthy incisors were studied: a control group and two groups pre-treated with salivary peptides before being demineralized, allowing for a comparison of enamel texture.
  • The study found that peptide-treated samples exhibited greater texture variations and multiple orientation populations of hydroxyapatite crystals, highlighting the potential of EDLD for detailed analysis in dental research.
View Article and Find Full Text PDF

Introduction: Statherin-derived peptide (StatpSpS) has shown promise against erosive tooth wear. To elucidate its interaction with the hydroxyapatite (HAP) surface, the mechanism related to adsorption of this peptide with HAP was investigated through nanosecond-long all-atom molecular dynamics simulations.

Methods: StatpSpS was positioned parallel to the HAP surface in 2 orientations: 1 - neutral and negative residues facing the surface and 2 - positive residues facing the surface.

View Article and Find Full Text PDF

Background: We previously showed that fimbriae-bore from Poryphyromonas gingivalis (Pg), one of the putative periodontopathogenic bacteria specifically bound to a peptide domain (stat23, prp21) shared on statherin or acidic proline-rich protein 1 (PRP1) molecule of human salivary proteins (HSPs). Here, we investigated whether the nasal administration of DNA plasmid expressing Flt3 ligand (pFL) and CpG oligodeoxynucleotide 1826 as double DNA adjuvant (dDA) with stat23 and prpr21 induces antigen (Ag)-specific salivary secretory IgA (SIgA) antibodies (Abs) in mice. Further, we examined that stat23- and prpr21-specific salivary SIgA Abs induced by dDA have an impact on Pg-binding to human whole saliva-coated hydroxyapatite beads (wsHAPs).

View Article and Find Full Text PDF

Poly-γ-glutamic acid (γ-PGA) is a bio-derived water-soluble, edible, non-immunogenic nylon-like polymer with the biochemical characteristics of a polypeptide. This Bacillus-derived material has great potential for a wide range of applications, from bioremediation to tunable drug delivery systems. In the context of oral care, γ-PGA holds great promise in enamel demineralisation prevention.

View Article and Find Full Text PDF

Since the modification of the proteinaceous components of the Acquired Enamel Pellicle (AEP) could influence the adhesion of the most cariogenic bacteria, to dental surfaces, we assessed if engineered salivary peptides would affect the adherence and modulate the bacterial proteome upon adherence. Single-component AEPs were formed onto hydroxyapatite (HAp) discs by incubating them with statherin, histatin-3, DR9, DR9-DR9, DR9-RR14, RR14, and parotid saliva. Then, the discs were inoculated with UA159 and the bacteria were allowed to adhere for 2 h, 4 h, and 8 h ( = 12/treatment/time point).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!