A binding-to-release strategy for targeted anticancer drug delivery
Drug conjugates, such as antibody–drug conjugates (ADCs) and small molecule–drug conjugates (SMDCs), are often dependent on efficient receptor-mediated endocytosis for payload release1–3—supported by about 10% of targets4–7. For poorly internalizing targets, drug conjugates dissociate and clear rapidly, limiting efficacy. To overcome the limitation in the internalization-to-release (ITR) pattern, we introduce a binding-to-release (BTR) strategy that decouples drug release from endocytosis by positioning an electrophile for direct cleavage by a proximal nucleophilic residue within the binding pocket. To realize this, we developed phosphorus(V)–phenol exchange (PhoPEx), a sulfur(VI) fluoride exchange-inspired chemistry enabling release of various payloads. This platform demonstrated high specificity from in vitro to clinical specimens, achieving precise detection of fibroblast activation protein (FAP) expression in patient-derived lymph nodes. In therapeutic settings, the FAP-BTR-SMDC achieved 5.9-fold higher monomethyl auristatin E exposure (AUC0–120 h) in tumours than internalization-dependent FAP-ITR-SMDC, matching FAP-ITR-ADC levels while minimizing off-target release. This led to improved ratios: the tumour-to-blood ratio was 14.7- and 3.6-fold higher than that of FAP-ITR-SMDC and FAP-ITR-ADC, respectively, and the tumour-to-liver ratio was 55.1- and 58.7-fold higher, respectively. This biodistribution increased the maximum tolerated dose and led to near-complete tumour regression in various tumour models. We further extended BTR to programmed cell death ligand 1 (PD-L1) and an mRNA-display-derived FAP peptide, suggesting potential broad applicability. This work establishes a framework that overcomes the internalization barrier, broadening the target scope for therapeutic and diagnostic conjugates. A binding-to-release drug conjugate strategy enables targeted payload release without cellular internalization, improving tumour specificity, efficacy and expanding therapeutic targets beyond conventional drug conjugates.
Authors
- Changlun Wang
- Yanzhao Liu
- Mengxin Xu (ORCID: https://orcid.org/0000-0002-3826-7371)
- Xi‐Yang Cui (ORCID: https://orcid.org/0009-0002-9406-4680)
- Tianyi Cen
- Ziren Kong (ORCID: https://orcid.org/0000-0001-6588-4757)
- Yuedan Zheng
- Junyi Chen (ORCID: https://orcid.org/0000-0002-8129-1473)
- Zihao Wen
- Qiang Xu (ORCID: https://orcid.org/0009-0006-0491-467X)
- Da Xu
- Zhibo Liu (ORCID: https://orcid.org/0000-0002-1438-0062)
- Pei Liu
- Zijun Yan
- Zichen Gu
- Yupeng Wang
- Xinwei Li
- Yaping Luo
Institutions
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- Peking University (CN)
- Peking Union Medical College Hospital (CN)
- Beijing VDJBio (China) (CN)
- Beijing National Laboratory for Molecular Sciences (CN)
- Chengdu University (CN)
- State Key Laboratory of Synthetic Chemistry (CN)
- Ministry of Education (ET)
- Center for Life Sciences (CN)
- China National Petroleum Corporation (China) (CN)
Publication Details
- Journal
- Nature
- Published
- 2026-08-26
- DOI
- https://doi.org/10.1038/s41586-026-10971-0
- Primary Topic
- Peptidase Inhibition and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00