Evidence map›Paper›PMID 41298394›Full record

ArticleNature communications2025

Highly efficient and long-acting split-and-mix proteolysis targeting chimera based on self-assembled polylactic acid.

Mei-Miao Zhan, Hailing Chen, Meiling He, Chunli Song, Zijun Jiao, Na Liu, Zhihong Liu, Zhanfeng Hou, Ying Chen, Zhibo Song and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Supramolecular Degraders: An Emerging Paradigm in Targeted Protein Degradation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  4. Review
  5. Review
  6. 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

13 authors.

Mei-Miao Zhan *Pingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, China.
Hailing Chen *State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Meiling HeState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Chunli SongState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Zijun JiaoState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Na LiuState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Zhihong LiuPingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, China.
Zhanfeng HouState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Ying ChenPingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, China.
Zhibo SongSchool of Advanced Material, Peking University Shenzhen Graduate School, Shenzhen, China.
Yun XingState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Zigang LiPingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, China. lizg@pkusz.edu.cn.ORCID http://orcid.org/0000-0002-4649-1592
Feng YinPingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, China. yinfeng@szbl.ac.cn.

Funding

National Natural Science Foundation of China (National Science Foundation of China) 21933004;21977010;22307081;21977011;22307084
6 · The paper itself

Abstract

Proteolysis targeting chimera (PROTAC) technology has received extensive attention due to its "event-driven" mechanism of action. However, existing chimera molecules tend to have higher molecular weight and higher polar surface area and exhibit lower druggable properties. In order to effectively improve the bioavailability, circulation time and other proprietary drug parameters of "chimera molecules", we combine the characteristics of nanotechnology and chimera technology, and propose the strategy of "Split-and-Mix" proteolysis degradation (SM-PROTAC) technology. However, both peptide- and liposome-based SM-PROTAC showed suboptimal in vivo efficiency. Hence, in this study, we incorporated Polylactic acid (PLA), an FDA-approved biomedical material, as the self-assembled matrix for SM-PROTAC to enhance in vivo effectiveness. PLA-based SM-PROTACs successfully degrade model targets including BRD4, ERα, and CDK4 in cellular assays and display more obvious tumor inhibition in vivo in female mice with a lower target ligand content (~1/10 of small molecule PROTAC controls) and long-term therapeutic potential (1 injection per three days vs 1 injection every day). In summary, PLA-based SM-PROTACs demonstrate promising drug characteristics and present obvious advantages in low-dose and long-term applications, providing additional insights into the pharmaceutical potential of the SM-PROTAC strategy.

Indexed as

PolyestersProteolysisAnimalsCell Line, TumorFemaleHumansMiceMice, Inbred BALB CProteolysis Targeting ChimeraPolyesterspoly(lactide)Proteolysis Targeting Chimera

Identifiers

PMID41298394
PMCPMC12658001

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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.