Evidence map›Paper›PMID 27982100›Full record

ArticleScientific reports2016

Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates.

Vanessa Siegmund, Birgit Piater, Bijan Zakeri, Thomas Eichhorn, Frank Fischer, Carl Deutsch, Stefan Becker, Lars Toleikis, Björn Hock, Ulrich A K Betz and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation.Journal of the American Chemical Society · 2025
    Article
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  17. Improving theranostics in pancreatic cancer.Journal of surgical oncology · 2017
    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

11 authors at 3 institutions in 2 countries.

Vanessa SiegmundInstitute of Organic Chemistry and Biochemistry, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Birgit PiaterMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Bijan ZakeriEMD Serono Research &Development Institute, Inc., 45A Middlesex Turnpike, Billerica, MA 01821, USA.
Thomas EichhornMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Frank FischerMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Carl DeutschMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Stefan BeckerMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Lars ToleikisMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Björn HockMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Ulrich A K BetzMerck KGaA, Frankfurter Straße 250, 64293 Darmstadt, Germany.
Harald KolmarInstitute of Organic Chemistry and Biochemistry, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Merck (Germany) · DETechnical University of Darmstadt · DEOno Pharmaceutical (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spontaneous isopeptide bond formation, a stabilizing posttranslational modification that can be found in gram-positive bacterial cell surface proteins, has previously been used to develop a peptide-peptide ligation technology that enables the polymerization of tagged-proteins catalyzed by SpyLigase. Here we adapted this technology to establish a novel modular antibody labeling approach which is based on isopeptide bond formation between two recognition peptides, SpyTag and KTag. Our labeling strategy allows the attachment of a reporting cargo of interest to an antibody scaffold by fusing it chemically to KTag, available via semi-automated solid-phase peptide synthesis (SPPS), while equipping the antibody with SpyTag. This strategy was successfully used to engineer site-specific antibody-drug conjugates (ADCs) that exhibit cytotoxicities in the subnanomolar range. Our approach may lead to a new class of antibody conjugates based on peptide-tags that have minimal effects on protein structure and function, thus expanding the toolbox of site-specific antibody conjugation.

Indexed as

AntibodiesChemical EngineeringImmunoconjugatesPeptidesPharmaceutical PreparationsTechnology, PharmaceuticalAntibodiesImmunoconjugatesPeptidesPharmaceutical Preparations

Identifiers

PMID27982100
PMCPMC5159917
OpenAlexW2565374594

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.