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0 reviewsSUMMARYPassive diffusion does not explain why many drugs are too large and/or too polar for rule-breaking membranepenetration, such as proteolysis-targeting chimeras (PROTACs, generally of a molecular weight > 800 Da).Here, using biotinylated chemical-probe-based target fishing and genetic knockdown/knockin approaches,we discovered that the membrane cluster of differentiation 36 (CD36) binds to and facilitates the uptake andefficacy of diverse PROTACs (e.g., SIM1-Me, MZ1, and clinical ARV-110) and large and/or polar small-molecule drugs (e.g., rapalink-1, rapamycin, navitoclax, birinapant, tubacin, and doxorubicin) via the CD36-mediated early endosome antigen 1 (EEA1)/Ras-related protein 5A (Rab5) endosomal cascade in vitro and/orin vivo. We then devised a novel chemical endocytic medicinal chemistry strategy to improve binding ofPROTACs to CD36 using structural modifications via the prodrug approach, markedly enhancing PROTACanti-tumor efficacy through spontaneously augmenting permeability and solubility
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