Gel filtration, ion exchange chromatography and chemical analysis of macromolecules present in acquired anamel pellicle (2‐hour‐pellicle)

Eggen, Kirsten Hannesson; Rölla, Gunnar

doi:10.1111/j.1600-0722.1982.tb00725.x

Cited by 22 publications

(29 citation statements)

References 17 publications

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“…The repulsive DLVO forces have their origin in the confinement of cationic counterions; the absence of the repulsion implies neutralisation or strong screening of the negative mica surface charge by the adsorbed salivary film, and therefore that the material that adsorbs to the mica must have been net positively charged. This contrasts with previous work (Eggen and Ro¨lla 1982) that showed an in vivo pellicle on hydroxyapatite to be made up of predominantly anionic material. An absence of long-ranged DLVO effects has been noted in an earlier colloidal-probe AFM study of the adsorbed salivary film (Hahn , using silica substrata.…”

Section: Normal Forces Sal-icontrasting

confidence: 99%

Lubrication and load-bearing properties of human salivary pellicles adsorbed ex vivo on molecularly smooth substrata

et al. 2012

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In a series of Surface Force Balance experiments, material from human whole saliva was adsorbed to molecularly smooth mica substrata (to form an 'adsorbed salivary film'). Measurements were taken of normal (load bearing, F n ) and shear (frictional, F s *) forces between two interacting surfaces. One investigation involved a salivary film formed by overnight adsorption from undiluted, centrifuged saliva, with the adsorbed film rinsed with pure water before measurement. Measurements were taken under pure water and 70 mM NaNO 3 . In a second investigation, a film was formed from and measured under a solution of 7% filtered saliva in 10 mM NaNO 3 . F n results for both systems showed purely repulsive layers, with an uncompressed thickness of 35-70 nm for the diluted saliva investigation and, prior to the application of shear, 11 nm for the rinsed system. F s * was essentially proportional to F n for all systems and independent of shear speed (in the range 100-2000 nm s 71 ), with coefficients of friction m * 0.24 and m * 0.46 for the unrinsed and rinsed systems, respectively. All properties of the rinsed system remained similar when the pure water measurement environment was changed to 70 mM NaNO 3 . For all systems studied, shear gave rise to an approximately threefold increase in the range of normal forces, attributed to the ploughing up of adsorbed material during shear to form debris that stood proud of the adsorbed layer. The results provide a microscopic demonstration of the wear process for a salivary film under shear and may be of particular interest for understanding the implications for in vivo oral lubrication under conditions such as rinsing of the mouth cavity. The work is interpreted in light of earlier studies that showed a structural collapse and increase in friction for an adsorbed salivary film in an environment of low ionic strength.

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Section: Normal Forces Sal-icontrasting

confidence: 99%

Lubrication and load-bearing properties of human salivary pellicles adsorbed ex vivo on molecularly smooth substrata

et al. 2012

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“…A possible additional factor is the ability of STP to chelate calcium, since calcium ions are believed to be important in the adhesion of anionic proteins to the surface of HA 5 and in maintaining the cohesion of pellicle. 29 The relatively greater importance of surface charge effects is possibly suggested by observations that adsorption of proteins to HA is reduced, and desorption increased, by both chelating and non-chelating anions, including fluoride, 5 pyrophosphate, 10,11 trimetaphosphate, 9 diphosphonates, 12 glycerophosphate 30 and phytic acid. 30 In agreement with previous work we found that orthophosphate promoted protein desorption 5 but did not inhibit adsorption.…”

Section: Discussionmentioning

confidence: 99%

In vitro studies on the effect of sodium tripolyphosphate on the interactions of stain and salivary protein with hydroxyapatite

Shellis

Addy

Rees

2005

Journal of Dentistry

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“…Since the pellicle material harvested from human teeth is scarce, several studies have been performed through the incubation of whole saliva with HA powder [6, 15, 19 -23] or HA plaques [24,25] in vitro conditions. Pertaining to in vivo studies, several strategies have been used to obtain AEP namely: scraping the buc-cal surfaces with coromant scaler [18,26]; rubbing each teeth surface with sponges containing SDS solution [6]; using Durapore membrane filters [15, 27 -29]; fixing bovine enamel on the teeth surface [30 -32] and more recently using a dry collection strip (electrode wick paper filter) [33]. Identification of AEP protein components has been carried out by different technical approaches showing the presence of acidic PRPs [5,6,29,34] statherin, histatins, amylase, carbonic anhydrase VI, lactoferrin, mucins (MG1 and MG2), lysozyme and cystatins [6,28,29,31,32,34,35].…”

Section: Introductionmentioning

confidence: 99%

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

Vitorino

Calheiros-Lobo²,

Duarte

et al. 2008

J of Separation Science

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The present study proposes a strategy for human in vivo acquired enamel pellicle (AEP) peptidome characterisation based on sequential extraction with guanidine and TFA followed by MALDI-TOF/TOF identification. Three different nanoscale analytical approaches were used: samples were subjected to tryptic digestion followed by nano-HPLC and mass spectrometry (MS and MS/MS) analysis. Undigested samples were analysed by LC-MS (both linear and reflector modes) and LC-MS/MS analysis, and samples were subjected to nano-HPLC followed by on-plate digestion and mass spectrometry (MS and MS/MS) analysis. The majority of the identifications corresponded to peptide/protein fragments of salivary protein, belonging to the classes: acidic PRPs, basic PRPs, statherin, cystatins S and SN and histatin 1 (all also identified in intact form). Overall, more than 90 peptides/proteins were identified. Results clearly show that peptides with acidic groups are enriched in the TFA fraction while peptides with no acidic or phosphate groups are prevalent on the guanidine extract. Also, phosphorylated peptides were observed mainly on the TFA fraction. Fragments present in the AEP show a predominance of cleavage points located at Arg, Tyr and Lys residues. Obtained data suggest that proteolytic activity could influence AEP formation and composition.

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Gel filtration, ion exchange chromatography and chemical analysis of macromolecules present in acquired anamel pellicle (2‐hour‐pellicle)

Cited by 22 publications

References 17 publications

Lubrication and load-bearing properties of human salivary pellicles adsorbed ex vivo on molecularly smooth substrata

Lubrication and load-bearing properties of human salivary pellicles adsorbed ex vivo on molecularly smooth substrata

In vitro studies on the effect of sodium tripolyphosphate on the interactions of stain and salivary protein with hydroxyapatite

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

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