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The major obstacles to triple‐negative breast cancer (TNBC) therapy are metastasis and mortality rates, leading to the failure treatment of traditional chemotherapy. Therefore, low toxicity drugs and more effective therapeutic approaches are greatly desired. Considering the drawbacks of indocyanine green (ICG) and purpurin such as poor bioavailability and rapid blood clearance, an endogenous carrier material human serum albumin (HSA) was employed to construct the nanoplatform through hydrophobic interaction with the inspiration of successful delivery of paclitaxel. Herein, we developed and fabricated a new self‐assembled albumin‐based drug delivery system (ICG‐purpurin@HSA, HIP) with encapsulation of ICG and purpurin. Of note, compared to free ICG and purpurin, enhanced treatment efficiency was achieved by the HIP with the help of reactive oxygen species (ROS)‐heat‐induced damage and nutrient supply cutoff. Consequently, an efficient drug delivery platform based on photothermal therapy (PTT) and photodynamic therapy (PDT) was proposed, revealing a promising strategy for TNBC treatment. [ABSTRACT FROM AUTHOR]

The periodic twist behaviors of amyloid fibrils initiated and formed on block copolymer films with nanoscale features are studied. The discovery of twist variations even in a single amyloid fibril is reported: the fibril can vary its twist extents in response to the underlying nanopatterned surfaces by keeping its neighboring crossover sections right above the periodic nanodomains and tuning the distance between neighboring crossover sections based on either the periodic nanodomain distance or the fibril contour direction. This nanopattern‐induced twist polymorphism arises from the fibril's two edges, exhibiting different hydrophobic interactions with the periodic nanodomains, as demonstrated by simulation studies. This work contributes to the understanding of surface effects on twist polymorphism in amyloid fibril structures that may be important to fibril polymorphism in amyloid pathologies and bioapplications of amyloid fibrils. [ABSTRACT FROM AUTHOR]