Evidence map›Paper›PMID 36834935›Full record

ReviewInternational journal of molecular sciences2023

bioTCIs: Middle-to-Macro Biomolecular Targeted Covalent Inhibitors Possessing Both Semi-Permanent Drug Action and Stringent Target Specificity as Potential Antibody Replacements.

Jay Yang, Yudai Tabuchi, Riku Katsuki, Masumi Taki

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. 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
1.4field-weighted citation impact, top 20% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Selection of antibody-binding covalent aptamers.Communications chemistry · 2024
    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

4 authors at 3 institutions in 2 countries.

Jay YangDepartment of Engineering Science, Graduate School of Informatics and Engineering, University of Electro-Communications (UEC), 1-5-1 Chofugaoka, Chofu 182-8585, Japan.ORCID 0000-0003-1621-0486
Yudai TabuchiDepartment of Engineering Science, Graduate School of Informatics and Engineering, University of Electro-Communications (UEC), 1-5-1 Chofugaoka, Chofu 182-8585, Japan.
Riku KatsukiDepartment of Engineering Science, Graduate School of Informatics and Engineering, University of Electro-Communications (UEC), 1-5-1 Chofugaoka, Chofu 182-8585, Japan.
Masumi TakiDepartment of Engineering Science, Graduate School of Informatics and Engineering, University of Electro-Communications (UEC), 1-5-1 Chofugaoka, Chofu 182-8585, Japan.ORCID 0000-0002-1811-8029
University of Electro-Communications · JPThe Graduate University for Advanced Studies, SOKENDAI · JPUniversity of Wisconsin–Madison · US

Funding

Japan Society for the Promotion of Science 20J22890Japan Society for the Promotion of Science 21K05287
6 · The paper itself

Abstract

Monoclonal antibody therapies targeting immuno-modulatory targets such as checkpoint proteins, chemokines, and cytokines have made significant impact in several areas, including cancer, inflammatory disease, and infection. However, antibodies are complex biologics with well-known limitations, including high cost for development and production, immunogenicity, a limited shelf-life because of aggregation, denaturation, and fragmentation of the large protein. Drug modalities such as peptides and nucleic acid aptamers showing high-affinity and highly selective interaction with the target protein have been proposed alternatives to therapeutic antibodies. The fundamental limitation of short in vivo half-life has prevented the wide acceptance of these alternatives. Covalent drugs, also known as targeted covalent inhibitors (TCIs), form permanent bonds to target proteins and, in theory, eternally exert the drug action, circumventing the pharmacokinetic limitation of other antibody alternatives. The TCI drug platform, too, has been slow in gaining acceptance because of its potential prolonged side-effect from off-target covalent binding. To avoid the potential risks of irreversible adverse drug effects from off-target conjugation, the TCI modality is broadening from the conventional small molecules to larger biomolecules possessing desirable properties (e.g., hydrolysis resistance, drug-action reversal, unique pharmacokinetics, stringent target specificity, and inhibition of protein-protein interactions). Here, we review the historical development of the TCI made of bio-oligomers/polymers (i.e., peptide-, protein-, or nucleic-acid-type) obtained by rational design and combinatorial screening. The structural optimization of the reactive warheads and incorporation into the targeted biomolecules enabling a highly selective covalent interaction between the TCI and the target protein is discussed. Through this review, we hope to highlight the middle to macro-molecular TCI platform as a realistic replacement for the antibody.

Indexed as

AntibodiesDrug DesignPharmaceutical PreparationsAntibodiesPharmaceutical Preparationscovalent aptamermatchmaking microenvironmentmiddle-molecule covalent drugpeptide/oligonucleotide therapeuticspharmacokinetic parameter (kinact/KI)protease/nuclease resistancequiescent affinity labelreactivity and affinity-based co-selectionreversing adverse drug effects (ADEs)warhead

Identifiers

PMID36834935
PMCPMC9968108
OpenAlexW4319922732

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.