Evidence map›Paper›PMID 38737471›Full record

ArticleMedComm2024

Half-life extension of single-domain antibody-drug conjugates by albumin binding moiety enhances antitumor efficacy.

Quanxiao Li, Yu Kong, Yuxuan Zhong, Ailing Huang, Tianlei Ying, Yanling Wu

Abstract read
In one paragraph

Article in MedComm, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  14. Radiotheranostic landscape: A review of clinical and preclinical development.European journal of nuclear medicine and molecular imaging · 2025
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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

6 authors.

Quanxiao LiMOE/NHC/CAMS Key Laboratory of Medical Molecular Virology Shanghai Institute of Infectious Disease and Biosecurity Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection Shanghai Engineering Research Center for Synthetic Immunology Department of medical microbiology and parasitology, School of Basic Medical Sciences Fudan University Shanghai China.
Yu KongMOE/NHC/CAMS Key Laboratory of Medical Molecular Virology Shanghai Institute of Infectious Disease and Biosecurity Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection Shanghai Engineering Research Center for Synthetic Immunology Department of medical microbiology and parasitology, School of Basic Medical Sciences Fudan University Shanghai China.
Yuxuan ZhongMOE/NHC/CAMS Key Laboratory of Medical Molecular Virology Shanghai Institute of Infectious Disease and Biosecurity Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection Shanghai Engineering Research Center for Synthetic Immunology Department of medical microbiology and parasitology, School of Basic Medical Sciences Fudan University Shanghai China.
Ailing HuangCollege of Life Sciences Hebei Agricultural University Baoding China.
Tianlei YingMOE/NHC/CAMS Key Laboratory of Medical Molecular Virology Shanghai Institute of Infectious Disease and Biosecurity Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection Shanghai Engineering Research Center for Synthetic Immunology Department of medical microbiology and parasitology, School of Basic Medical Sciences Fudan University Shanghai China.
Yanling WuMOE/NHC/CAMS Key Laboratory of Medical Molecular Virology Shanghai Institute of Infectious Disease and Biosecurity Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection Shanghai Engineering Research Center for Synthetic Immunology Department of medical microbiology and parasitology, School of Basic Medical Sciences Fudan University Shanghai China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-domain antibody-drug conjugates (sdADCs) have been proven to have deeper solid tumor penetration and intratumor accumulation capabilities due to their smaller size compared with traditional IgG format ADCs. However, one of the key challenges for improving clinical outcomes of sdADCs is their abbreviated in vivo half-life. In this study, we innovatively fused an antihuman serum albumin (αHSA) nanobody to a sdADCs targeting oncofetal antigen 5T4, conferring serum albumin binding to enhance the pharmacokinetic profiles of sdADCs. The fusion protein was conjugated with monomethyl auristatin E (MMAE) at s224c site mutation. The conjugate exhibited potent cytotoxicity against various tumor cells. Compared with the nonalbumin-binding counterparts, the conjugate exhibited a 10-fold extended half-life in wild-type mice and fivefold prolonged serum half-life in BxPC-3 xenograft tumor models as well as enhanced tumor accumulation and retention in mice. Consequently, n501-αHSA-MMAE showed potent antitumor effects, which were comparable to n501-MMAE in pancreatic cancer BxPC-3 xenograft tumor models; however, in human ovarian teratoma PA-1 xenograft tumor models, n501-αHSA-MMAE significantly improved antitumor efficacy. Moreover, the conjugate showed mitigated hepatotoxicity. In summary, our results suggested that fusion to albumin-binding moiety as a viable strategy can enhance the therapeutic potential of sdADCs through optimized pharmacokinetics.

Indexed as

albumin‐binding moietyantitumor efficacyhalf‐life extensionsingle‐domain antibody–drug conjugates

Identifiers

PMID38737471
PMCPMC11082534

What OpenQuestion holds

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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.