Evidence map›Paper›PMID 24668773›Full record

ArticleProtein engineering, design & selection : PEDS2014

Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications.

Christian Tiede, Anna A S Tang, Sarah E Deacon, Upasana Mandal, Joanne E Nettleship, Robin L Owen, Suja E George, David J Harrison, Raymond J Owens, Darren C Tomlinson and 1 more

Abstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Article
  2. Review
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  5. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
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  11. Automated Purification of DNA Origami with SPRI Beads.Small (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  12. Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

11 authors.

Christian TiedeBiomedical Health Research Centre, BioScreening Technology Group, University of Leeds, Leeds LS2 9JT, UK.
Anna A S Tang
Sarah E Deacon
Upasana Mandal
Joanne E Nettleship
Robin L Owen
Suja E George
David J Harrison
Raymond J Owens
Darren C Tomlinson
Michael J McPherson

Funding

Biotechnology and Biological Sciences Research Council 24/G15882Medical Research Council MR/K018779/1Wellcome Trust WT 088908/Z/09/Z
6 · The paper itself

Abstract

We have designed a novel non-antibody scaffold protein, termed Adhiron, based on a phytocystatin consensus sequence. The Adhiron scaffold shows high thermal stability (Tm ca. 101°C), and is expressed well in Escherichia coli. We have determined the X-ray crystal structure of the Adhiron scaffold to 1.75 Å resolution revealing a compact cystatin-like fold. We have constructed a phage-display library in this scaffold by insertion of two variable peptide regions. The library is of high quality and complexity comprising 1.3 × 10(10) clones. To demonstrate library efficacy, we screened against the yeast Small Ubiquitin-like Modifier (SUMO). In selected clones, variable region 1 often contained sequences homologous to the known SUMO interactive motif (V/I-X-V/I-V/I). Four Adhirons were further characterised and displayed low nanomolar affinities and high specificity for yeast SUMO with essentially no cross-reactivity to human SUMO protein isoforms. We have identified binders against >100 target molecules to date including as examples, a fibroblast growth factor (FGF1), platelet endothelial cell adhesion molecule (PECAM-1; CD31), the SH2 domain Grb2 and a 12-aa peptide. Adhirons are highly stable and well expressed allowing highly specific binding reagents to be selected for use in molecular recognition applications.

Indexed as

Peptide LibraryAmino Acid SequenceBase SequenceConsensus SequenceCystatinsHumansModels, MolecularMolecular Sequence DataPeptidesProtein EngineeringProtein StabilityProtein Structure, SecondarySUMO-1 ProteinTemperatureCystatinsPeptide LibraryPeptidesSUMO-1 Proteinconsensus proteinhigh specificity bindingnon-antibody-binding proteinprotein–protein interactionSUMO

Identifiers

PMID24668773
PMCPMC4000234

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Registered trials

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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.