Publications by authors named "Caili Luo"
Article Synopsis
- Researchers developed a new reversible modification method for proteins that can modify the N-terminal site, making it adaptable to 20 different amino acids and applicable under biologically relevant conditions.
- This strategy allows for the switchable manipulation of proteins, including complex substrates like antibodies, enabling efficient release of native proteins through a deconjugation process.
- The approach offers promising applications in chemical biology and medicinal research by allowing precise control over protein function and enhancing techniques like proteomics analysis.
The approval of Trodelvy® validates TROP2 as a druggable but challenging target for antibody-drug conjugates (ADCs) to treat metastatic triple-negative breast cancer (mTNBC). Here, based on the TROP2-targeted antibody sacituzumab, we designed and developed several site-specific ADC candidates, which employ MMAE (monomethyl auristatin E) as the toxin, via IgG glycoengineering or affinity-directed traceless conjugation. Systematic evaluation of these site-specific ADCs in homogeneity, hydrophilicity, stability, and antitumor efficiency was conducted.
View Article and Find Full Text PDFThe inadequate understanding of the structure-activity relationship (SAR) of glycosite-specific antibody-drug conjugates (ADCs) hinders its design and development. Herein, we revealed the systemic SAR and structure-toxicity relationship (STR) of gsADCs by constructing 50 gsADC structures bearing three glycan subtypes and diverse linker-drug combinations. According to the results, extra hydrophilic linkers are indispensable for the intact glycan-based gsADCs to achieve better efficacy.
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