Evidence map›Paper›PMID 23728098›Full record

ArticleCellular and molecular life sciences : CMLS2013

Development and characterization of small bispecific albumin-binding domains with high affinity for ErbB3.

Johan Nilvebrant, Mikael Astrand, John Löfblom, Sophia Hober

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. [EJNMMI research · 2020
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  11. The albumin-binding domain as a scaffold for protein engineering.Computational and structural biotechnology journal · 2013
    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

4 authors at 2 institutions in 1 country.

Johan NilvebrantDivision of Protein Technology, KTH Royal Institute of Technology, AlbaNova University Center, 106 91, Stockholm, Sweden.
Mikael Astrand
John Löfblom
Sophia Hober
AlbaNova · SEKTH Royal Institute of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Affinity proteins based on small scaffolds are currently emerging as alternatives to antibodies for therapy. Similarly to antibodies, they can be engineered to have high affinity for specific proteins. A potential problem with small proteins and peptides is their short in vivo circulation time, which might limit the therapeutic efficacy. To circumvent this issue, we have engineered bispecificity into an albumin-binding domain (ABD) derived from streptococcal Protein G. The inherent albumin binding was preserved while the opposite side of the molecule was randomized for selection of high-affinity binders. Here we present novel ABD variants with the ability to bind to the epidermal growth factor receptor 3 (ErbB3). Isolated candidates were shown to have an extraordinary thermal stability and affinity for ErbB3 in the nanomolar range. Importantly, they were also shown to retain their affinity to albumin, hence demonstrating that the intended strategy to engineer bispecific single-domain proteins against a tumor-associated receptor was successful. Moreover, competition assays revealed that the new binders could block the natural ligand Neuregulin-1 from binding to ErbB3, indicating a potential anti-proliferative effect. These new binders thus represent promising candidates for further development into ErbB3-signaling inhibitors, where the albumin interaction could result in prolonged in vivo half-life.

Indexed as

Bacterial ProteinsBinding, CompetitiveBiosensing TechniquesEscherichia coliHumansLigandsNerve Growth FactorsPeptide LibraryProtein BindingProtein Interaction Domains and MotifsProtein StabilityProtein Structure, SecondaryReceptor, ErbB-3Serum AlbuminSerum Albumin, HumanTemperatureALB protein, humanBacterial ProteinsERBB3 protein, humanIgG Fc-binding protein, StreptococcusLigandsNerve Growth FactorsNRG2 protein, humanPeptide LibraryReceptor, ErbB-3Serum AlbuminSerum Albumin, Human

Identifiers

PMID23728098
PMCPMC11113916
OpenAlexW2027155177

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.