Evidence map›Paper›PMID 26749427›Full record

ArticleAngewandte Chemie (International ed. in English)2016

iBodies: Modular Synthetic Antibody Mimetics Based on Hydrophilic Polymers Decorated with Functional Moieties.

Pavel Šácha, Tomáš Knedlík, Jiří Schimer, Jan Tykvart, Jan Parolek, Václav Navrátil, Petra Dvořáková, František Sedlák, Karel Ulbrich, Jiří Strohalm and 3 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

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  11. Artificial antibody created by conformational reconstruction of the complementary-determining region on gold nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

13 authors.

Pavel ŠáchaInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Tomáš KnedlíkInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Jiří SchimerInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Jan TykvartInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Jan ParolekInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Václav NavrátilInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Petra DvořákováInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
František SedlákInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Karel UlbrichInstitute of Macromolecular Chemistry, Academy of Science of the Czech Republic, Heyrovského n. 2, 16206, Prague 6, Czech Republic.
Jiří StrohalmInstitute of Macromolecular Chemistry, Academy of Science of the Czech Republic, Heyrovského n. 2, 16206, Prague 6, Czech Republic.
Pavel MajerInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic.
Vladimír ŠubrInstitute of Macromolecular Chemistry, Academy of Science of the Czech Republic, Heyrovského n. 2, 16206, Prague 6, Czech Republic. subr@imc.cas.cz.
Jan KonvalinkaInstitute of Organic Chemistry and Biochemistry, Academy of Science of the Czech Republic, Flemingovo n. 2, 16610, Prague 6, Czech Republic. konval@uochb.cas.cz.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies are indispensable tools for biomedicine and anticancer therapy. Nevertheless, their use is compromised by high production costs, limited stability, and difficulty of chemical modification. The design and preparation of synthetic polymer conjugates capable of replacing antibodies in biomedical applications such as ELISA, flow cytometry, immunocytochemistry, and immunoprecipitation is reported. The conjugates, named "iBodies", consist of an HPMA copolymer decorated with low-molecular-weight compounds that function as targeting ligands, affinity anchors, and imaging probes. We prepared specific conjugates targeting several proteins with known ligands and used these iBodies for enzyme inhibition, protein isolation, immobilization, quantification, and live-cell imaging. Our data indicate that this highly modular and versatile polymer system can be used to produce inexpensive and stable antibody substitutes directed toward virtually any protein of interest with a known ligand.

Indexed as

Molecular MimicryAntibodiesCell Line, TumorHumansHydrophobic and Hydrophilic InteractionsPolymersAntibodiesPolymersantibody mimeticsHPMAmolecular recognitionpolymer conjugatesprotein targeting

Identifiers

PMID26749427
PMCPMC4755222

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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.