Circulating tumor cells (CTCs) have been recognized as significant research target for cancer prognosis and metastasis mechanism. Efficient and all‐subpopulations‐covered isolation and facile release of CTCs with good viability are pivotal for profound mechanism research and molecular profiling. However, integrated nanoplatform with these two functions is yet to be elucidated. Among existing release techniques including physical, biological, and chemical methods, acid responsive release of CTCs attracts intensive interests due to its straightforward and easily accessible feature. However, extra acidic substance seems indispensable so far, which poses potential hazard to the rare and susceptible CTCs. To address this challenge, polyelectrolyte functionalized CaCO3 coated magnetic nanocrystal clusters are developed as the nanoplatform for multi‐subpopulations isolation and pH‐sensitive release of CTCs. Only buffer solution components are needed rather than other acidic substance to provide mild acidic environment with pH value of 6.5, facilitate highly efficient release. Moreover, the bioefficacy of CTC capture and mild condition recovery is not compromised by formation of protein corona on the cell‐friendly nanoplatform. This nanoplatform exhibits good performance in both mimic blood samples and cancer patients’ clinical samples.
An effective systemic mechanism regulates tumor development and progression; thus, a rational design in a one‐stone‐two‐birds strategy is meant for cancer treatment. Herein, a hollow Fe3O4 catalytic nanozyme carrier co‐loading lactate oxidase (LOD) and a clinically‐used hypotensor syrosingopine (Syr) are developed and delivered for synergetic cancer treatment by augmented self‐replenishing nanocatalytic reaction, integrated starvation therapy, and reactivating anti‐tumor immune microenvironment. The synergetic bio‐effects of this nanoplatform stemmed from the effective inhibition of lactate efflux through blocking the monocarboxylate transporters MCT1/MCT4 functions by the loaded Syr as a trigger. Sustainable production of hydrogen peroxide by catalyzation of the increasingly residual intracellular lactic acid by the co‐delivered LOD and intracellular acidification enabled the augmented self‐replenishing nanocatalytic reaction. Large amounts of produced reactive oxygen species (ROS) damaged mitochondria to inhibit oxidative phosphorylation as the substituted energy supply upon the hampered glycolysis pathway of tumor cells. Meanwhile, remodeling anti‐tumor immune microenvironment is implemented by pH gradient reversal, promoting the release of proinflammatory cytokines, restored effector T and NK cells, increased M1‐polarize tumor‐associated macrophages, and restriction of regulatory T cells. Thus, the biocompatible nanozyme platform achieved the synergy of chemodynamic/immuno/starvation therapies. This proof‐of‐concept study represents a promising candidate nanoplatform for synergetic cancer treatment.
Anisotropic self-assembly of nanoparticles (NPs) stems from the fine-tuning of their surface functionality and NP interaction. Strategies involving ligand interaction, protein interaction, and external stimulus have been developed. However, robust construction of monodispersed magnetic NPs to tens of microns of anisotropically aligned colloidal assembly triggered by adsorbed protein intermolecular interaction is yet to be elucidated. Here, we present the NP–protein interaction, magnetic force, and protein corona intermolecular interaction serially but independently induced path-dependent self-assembly of 100 nm Fe3O4@SiO2 nanocomposites. Dynamic formation of the micron-sized anisotropic magnetic assembly was reproducibly realized in a continuous medium in a controllable manner. Formation of the primary globular clusters upon the unique NP–protein complexes with the help of ions acts as the prerequisite for the anisotropic colloidal assembly, followed by the magnetic force-driven pre-organization and protein intermolecular electrostatic interaction-mediated elongation. The protein concentration rather than the protein original structure plays a more pivotal role in the NP–protein interaction and subsequent colloidal assembly process. Two typical serum proteins fibrinogen and bovine serum albumin enable formation of the anisotropic colloidal assembly but with a different subtle morphology. Furthermore, the obtained micron-sized magnetic colloidal assembly can be dissociated rapidly by adding a negative electrolyte in the medium due to the interference in the NP–protein interaction. However, the self-assembly process can be recycled based on the dissociated colloidal assembly.
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