In situ assembly of peptides in living cells.

A protocol enables in situ peptide self-assembly in living cells using stimuli-responsive unnatural amino acids, with glutathione- or sulfatase-triggered responsiveness and defined assembly conditions.

• Why it matters: Pre-assembled peptide nanostructures often show limited cellular uptake and low target selectivity, raising off-target risks and reducing therapeutic effectiveness. In situ assembly aims to improve internalization and local formation at target sites.
• What they did: The workflow covers peptide design and synthesis, then characterizes responsiveness to glutathione or sulfatase, followed by self-assembly testing in solution and in murine macrophage, human cervical carcinoma, and murine breast cancer cells. It also includes subcellular targeting and cancer therapy experiments in murine breast tumor-bearing BALB/c mice.
• The result: The described method provides a robust platform for developing in situ-formed peptide assemblies and supporting clinical translation of peptide-based supramolecular therapeutics, with an expected 92–115 d completion time.

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