Evidence map›Paper›PMID 36346602›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Antibody Affinity Maturation Using Computational Methods: From an Initial Hit to Small-Scale Expression of Optimized Binders.

Barbara Medagli, Miguel A Soler, Rita De Zorzi, Sara Fortuna

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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
–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

1 citing paper in PubMed.

  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

4 authors.

Barbara MedagliDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste, Italy. bmedagli@units.it.
Miguel A SolerCONCEPT Lab, Istituto Italiano di Tecnologia, Genova, Italy.
Rita De ZorziDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste, Italy.
Sara FortunaDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste, Italy. sara.fortuna@iit.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanobodies (VHHs) are engineered fragments of the camelid single-chain immunoglobulins. The VHH domain contains the highly variable segments responsible for antigen recognition. VHHs can be easily produced as recombinant proteins. Their small size is a good advantage for in silico approaches. Computer methods represent a valuable strategy for the optimization and improvement of their binding affinity. They also allow for epitope selection offering the possibility to design new VHHs for regions of a target protein that are not naturally immunogenic. Here we present an in silico mutagenic protocol developed to improve the binding affinity of nanobodies together with the first step of their in vitro production. The method, already proven successful in improving the low Kd of a nanobody hit obtained by panning, can be employed for the ex novo design of antibody fragments against selected protein target epitopes.

Indexed as

Single-Domain AntibodiesAntibody AffinityEpitopesRecombinant ProteinsEpitopesRecombinant ProteinsSingle-Domain AntibodiesAntigenBinding affinityIn silico protocolNanobodies (VHH)

Identifiers

PMID36346602

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.