Evidence map›Paper›PMID 33611612›Full record

ArticleEuropean biophysics journal : EBJ2021

Protein formulation through automated screening of pH and buffer conditions, using the Robotein® high throughput facility.

Ruth Kellner, Romain Malempré, Julie Vandenameele, Alain Brans, Anne-Françoise Hennen, Noémie Rochus, Alexandre Di Paolo, Marylène Vandevenne, André Matagne

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
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

9 authors at 2 institutions in 1 country.

Ruth KellnerLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium.
Romain MalempréLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium.
Julie VandenameeleLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium.
Alain BransLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium.
Anne-Françoise HennenEurogentec S.A., Rue Bois Saint-Jean, 5, 4102, Seraing, Belgium.
Noémie RochusEurogentec S.A., Rue Bois Saint-Jean, 5, 4102, Seraing, Belgium.
Alexandre Di PaoloEurogentec S.A., Rue Bois Saint-Jean, 5, 4102, Seraing, Belgium.
Marylène VandevenneLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium.
André MatagneLaboratory of Enzymology and Protein Folding, Centre for Protein Engineering, InBioS, University of Liège, Building B6C, Quartier Agora, Allée du 6 Août, 13, 4000, Liège (Sart-Tilman), Belgium. amatagne@ulg.ac.be.ORCID http://orcid.org/0000-0001-6417-6791
University of Liège · BEEurogentec (Belgium) · BE

Funding

Service Public de Wallonie 1510631
6 · The paper itself

Abstract

Among various factors, the direct environment (e.g. pH, buffer components, salts, additives, etc.…) is known to have a crucial effect on both the stability and activity of proteins. In particular, proper buffer and pH conditions can improve their stability and function significantly during purification, storage and handling, which is highly relevant for both academic and industrial applications. It can also promote data reproducibility, support the interpretation of experimental results and, finally, contribute to our general understanding of the biophysical properties of proteins. In this study, we have developed a high throughput screen of 158 different buffers/pH conditions in which we evaluated: (i) the protein stability, using differential scanning fluorimetry and (ii) the protein function, using either enzymatic assays or binding activity measurements, both in an automated manner. The modular setup of the screen allows for easy implementation of other characterization methods and parameters, as well as additional test conditions. The buffer/pH screen was validated with five different proteins used as models, i.e. two active-site serine β-lactamases, two metallo-β-lactamases (one of which is only active as a tetramer) and a single-domain dromedary antibody fragment (V

Indexed as

beta-LactamasesBuffersHydrogen-Ion ConcentrationProtein StabilityReproducibility of Resultsbeta-LactamasesBuffersBio-layer interferometryDifferential scanning fluorimetryHigh throughputNanobodyProtein formulationProtein stabilityβ-lactamases

Identifiers

PMID33611612
OpenAlexW3130741392

What OpenQuestion holds

Textmetadata
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.