Evidence map›Paper›PMID 26670810›Full record

ArticlePloS one2015

The Influence of Arginine on the Response of Enamel Matrix Derivative (EMD) Proteins to Thermal Stress: Towards Improving the Stability of EMD-Based Products.

Alessandra Apicella, Peggy Heunemann, Sreenath Bolisetty, Matteo Marascio, Anja Gemperli Graf, Laszlo Garamszegi, Raffaele Mezzenga, Peter Fischer, Christopher J Plummer, Jan-Anders Månson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.0field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Alessandra ApicellaLaboratoire des Technologie des Composites et Polymères (LTC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
Peggy HeunemannFood Process Engineering, Institute of Food, Nutrition and Health, ETH Zurich, 8092 Zurich, Switzerland.
Sreenath BolisettyFood and Soft Materials Science, Institute of Food, Nutrition and Health, ETH Zurich, 8092 Zurich, Switzerland.
Matteo MarascioLaboratoire des Technologie des Composites et Polymères (LTC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
Anja Gemperli GrafInstitut Straumann AG, 4052 Basel, Switzerland.
Laszlo GaramszegiInstitut Straumann AG, 4052 Basel, Switzerland.
Raffaele MezzengaFood and Soft Materials Science, Institute of Food, Nutrition and Health, ETH Zurich, 8092 Zurich, Switzerland.
Peter FischerFood Process Engineering, Institute of Food, Nutrition and Health, ETH Zurich, 8092 Zurich, Switzerland.
Christopher J PlummerLaboratoire des Technologie des Composites et Polymères (LTC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
Jan-Anders MånsonLaboratoire des Technologie des Composites et Polymères (LTC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
École Polytechnique Fédérale de Lausanne · CHETH Zurich · CHStraumann (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a current procedure for periodontal tissue regeneration, enamel matrix derivative (EMD), which is the active component, is mixed with a propylene glycol alginate (PGA) gel carrier and applied directly to the periodontal defect. Exposure of EMD to physiological conditions then causes it to precipitate. However, environmental changes during manufacture and storage may result in modifications to the conformation of the EMD proteins, and eventually premature phase separation of the gel and a loss in therapeutic effectiveness. The present work relates to efforts to improve the stability of EMD-based formulations such as Emdogain™ through the incorporation of arginine, a well-known protein stabilizer, but one that to our knowledge has not so far been considered for this purpose. Representative EMD-buffer solutions with and without arginine were analyzed by 3D-dynamic light scattering, UV-Vis spectroscopy, transmission electron microscopy and Fourier transform infrared spectroscopy at different acidic pH and temperatures, T, in order to simulate the effect of pH variations and thermal stress during manufacture and storage. The results provided evidence that arginine may indeed stabilize EMD against irreversible aggregation with respect to variations in pH and T under these conditions. Moreover, stopped-flow transmittance measurements indicated arginine addition not to suppress precipitation of EMD from either the buffers or the PGA gel carrier when the pH was raised to 7, a fundamental requirement for dental applications.

Indexed as

TemperatureArginineChemical PrecipitationDental Enamel ProteinsDynamic Light ScatteringHydrogen-Ion ConcentrationImaging, Three-DimensionalKineticsProtein ConformationSolutionsSpectrophotometry, UltravioletSpectroscopy, Fourier Transform InfraredStress, PhysiologicalArginineDental Enamel Proteinsenamel matrix proteinsSolutions

Identifiers

PMID26670810
PMCPMC4699454
OpenAlexW2204404639

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.