Evidence map›Paper›PMID 41378120›Full record

ReviewBiophysical reviews2025

Stabilising proteins in solution using affordable and readily available small molecules.

Sandrine Bakam Tchiakam, Sarah L Berger, June Southall, Helen Walden, Mads Gabrielsen

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2025. 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
–field-weighted citation impact
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.

  1. Article
  2. Biophysics in Great Britain and Ireland.Biophysical reviews · 2025
    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

5 authors.

Sandrine Bakam Tchiakam *School of Molecular Biosciences, University of Glasgow, Glasgow, G12 8QQ UK.
Sarah L Berger *School of Molecular Biosciences, University of Glasgow, Glasgow, G12 8QQ UK.
June SouthallNeil Bulleid Integrated Protein Analysis Facility, MVLS Shared Research Facilities, University of Glasgow, Glasgow, G12 8QQ UK.
Helen WaldenSchool of Molecular Biosciences, University of Glasgow, Glasgow, G12 8QQ UK.
Mads GabrielsenNeil Bulleid Integrated Protein Analysis Facility, MVLS Shared Research Facilities, University of Glasgow, Glasgow, G12 8QQ UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Purified proteins are sitting in a mostly aqueous environment, with normally some buffer and salt making up the conditions. This is vastly different from their natural habitat, and protein are often affected by this difference, showing signs of destabilisation or aggregation. A common method to improve the protein solubility and homogeneity is adding small molecules to the buffer conditions, as these can aid protein stability and keep the protein in solution at a concentration which is within that needed for the experiments that are to be undertaken. This review is detailing some of the small molecules that are routinely used, with a focus on them being readily available and affordable for all labs. Some of the more common small molecule additives described in this paper are (1) amino acids, like arginine or glycine, (2) sugars, like sucrose, or (3) other osmolytes, such as glycerol. The second part is covering some of the methods that can be utilised to determine whether a small molecule improves the stability of a particular protein.

Indexed as

Protein purificationProtein stabilitySmall molecule additives

Identifiers

PMID41378120
PMCPMC12686257

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.