Evidence map›Paper›PMID 33053650›Full record

ReviewInternational journal of molecular sciences2020

Toward Drug-Like Multispecific Antibodies by Design.

Manali S Sawant, Craig N Streu, Lina Wu, Peter M Tessier

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Engineered B7-H3 Binding in Modular Gp2 Miniproteins.Biotechnology and bioengineering · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. The Evolving Applications of Bispecific Antibodies: Reaping the Harvest of Early Sowing and Planting New Seeds.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  20. 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.

Manali S SawantDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA.
Craig N StreuDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA.
Lina WuBiointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Peter M TessierDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA.

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Design and Evolution of Polyvalent Domain Antibodies Specific for Tau AggregatesRF1AG059723 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KANE, RAVI S., TESSIER, PETER M · 2018 to 2022
$2.4M
Mechanisms transducing insulin and insulin resistance in the hippocampusR01AG050598 · NIA · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI MCNAY, EWAN C · 2016 to 2020
$1.9M
Structure-guided antibody targeting of pre-selected epitopes in amyloidogenic aggregatesR35GM136300 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESSIER, PETER M · 2020 to 2024
$1.5M
Design of Antibody Fragments Specific For Amyloidogenic AggregatesR01GM104130 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESSIER, PETER M · 2014 to 2018
$1.3M
NIA NIH HHS R01 AG050598NIA NIH HHS RF1 AG059723NIGMS NIH HHS R01 GM104130NIGMS NIH HHS R01GM104130NIGMS NIH HHS R35 GM136300NIGMS NIH HHS R35GM136300NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32-GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The success of antibody therapeutics is strongly influenced by their multifunctional nature that couples antigen recognition mediated by their variable regions with effector functions and half-life extension mediated by a subset of their constant regions. Nevertheless, the monospecific IgG format is not optimal for many therapeutic applications, and this has led to the design of a vast number of unique multispecific antibody formats that enable targeting of multiple antigens or multiple epitopes on the same antigen. Despite the diversity of these formats, a common challenge in generating multispecific antibodies is that they display suboptimal physical and chemical properties relative to conventional IgGs and are more difficult to develop into therapeutics. Here we review advances in the design and engineering of multispecific antibodies with drug-like properties, including favorable stability, solubility, viscosity, specificity and pharmacokinetic properties. We also highlight emerging experimental and computational methods for improving the next generation of multispecific antibodies, as well as their constituent antibody fragments, with natural IgG-like properties. Finally, we identify several outstanding challenges that need to be addressed to increase the success of multispecific antibodies in the clinic.

Indexed as

Antibody SpecificityDrug DesignProtein EngineeringAnimalsAntibodies, BispecificAntibodies, MonoclonalAntibody AffinityChemical PhenomenaDrug DevelopmentDrug StabilityHumansModels, MolecularSolubilityStructure-Activity RelationshipAntibodies, BispecificAntibodies, Monoclonalaffinityaggregationbispecificdevelopabilityimmunogenicitynon-specific bindingpharmacokineticspolyspecificityprotein engineeringself-associationsolubilityspecificitystabilityviscosity

Identifiers

PMID33053650
PMCPMC7589779

What OpenQuestion holds

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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.