Plasmon‐Enhanced Spectroscopies with Shell‐Isolated Nanoparticles

Shell‐isolated nanoparticle‐enhanced Raman spectroscopy (SHINERS), due to its versatility, has been able to break the long‐term limitations of the material‐ and substrate‐specific generalities in the traditional field of surface‐enhanced Raman spectroscopy. With a shell‐isolated work principle, this method provides an opportunity to investigate successfully in surface, biological systems, energetic materials, and environmental sciences. Both the shell material and core morphology are being improved continuously to meet the requirements in diverse systems, such as the electrochemical studies at single crystal electrode surfaces, in situ monitoring of photoinduced reaction processes, practical applications in energy conversion and storage, inspections in food safety, and the surface‐enhanced fluorescence. Predictably, the concept of shell‐isolated nanoparticle‐enhancement could be expanded to the wider range for the performance of plasmon‐enhanced spectral modifications.     

Ferritin Protein Regulates the Degradation of Iron Oxide Nanoparticles

Proteins implicated in iron homeostasis are assumed to be also involved in the cellular processing of iron oxide nanoparticles. In this work, the role of an endogenous iron storage protein—namely the ferritin—is examined in the remediation and biodegradation of magnetic iron oxide nanoparticles. Previous in vivo studies suggest the intracellular transfer of the iron ions released during the degradation of nanoparticles to endogenous protein cages within lysosomal compartments. Here, the capacity of ferritin cages to accommodate and store the degradation products of nanoparticles is investigated in vitro in the physiological acidic environment of the lysosomes. Moreover, it is questioned whether ferritin proteins can play an active role in the degradation of the nanoparticles. The magnetic, colloidal, and structural follow‐up of iron oxide nanoparticles and proteins in lysosome‐like medium confirms the efficient remediation of potentially harmful iron ions generated by nanoparticles within ferritins. The presence of ferritins, however, delays the degradation of particles due to a complex colloidal behavior of the mixture in acidic medium. This study exemplifies the important implications of intracellular proteins in processes of degradation and metabolization of iron oxide nanoparticles.     

Poly(N‐phenylglycine)‐Based Nanoparticles as Highly Effective and Targeted Near‐Infrared Photothermal Therapy/Photodynamic Therapeutic Agents for Malignant Melanoma

Malignant melanoma is a highly aggressive tumor resistant to chemotherapy. Therefore, the development of new highly effective therapeutic agents for the treatment of malignant melanoma is highly desirable. In this study, a new class of polymeric photothermal agents based on poly(N‐phenylglycine) (PNPG) suitable for use in near‐infrared (NIR) phototherapy of malignant melanoma is designed and developed. PNPG is obtained via polymerization of N‐phenylglycine (NPG). Carboxylate functionality of NPG allows building multifunctional systems using covalent bonding. This approach avoids complicated issues typically associated with preparation of polymeric photothermal agents. Moreover, PNPG skeleton exhibits pH‐responsive NIR absorption and an ability to generate reactive oxygen species, which makes its derivatives attractive photothermal therapy (PTT)/photodynamic therapy (PDT) dual‐modal agents with pH‐responsive features. PNPG is modified using hyaluronic acid (HA) and polyethylene glycol diamine (PEG‐diamine) acting as the coupling agent. The resultant HA‐modified PNPG (PNPG‐PEG‐HA) shows negligible cytotoxicity and effectively targets CD44‐overexpressing cancer cells. Furthermore, the results of in vitro and in vivo experiments reveal that PNPG‐PEG‐HA selectively kills B16 cells and suppresses malignant melanoma tumor growth upon exposure to NIR light (808 nm), indicating that PNPG‐PEG‐HA can serve as a very promising nanoplatform for targeted dual‐modality PTT/PDT of melanoma.     

Mild Binding of Protein to C2N Monolayer Reveals Its Suitable Biocompatibility

The development of biocompatible nanomaterials for smart drug delivery and bioimaging has attracted great interest in recent years in biomedical fields. Here, the interaction between the recently reported nitrogenated graphene (C₂N) and a prototypical protein (villin headpiece HP35) utilizing atomistic molecular dynamics simulations is studied. The simulations reveal that HP35 can form a stable binding with the C₂N monolayer. Although the C₂N–HP35 attractive interactions are constantly preserved, the binding strength between C₂N and the protein is mild and does not cause significant distortion in the protein's structural integrity. This intrinsic biofriendly property of native C₂N is distinct from several widely studied nanomaterials, such as graphene, carbon nanotubes, and MoS₂, which can induce severe protein denaturation. Interestingly, once the protein is adsorbed onto C₂N surface, its transverse migration is highly restricted at the binding sites. This restriction is orchestrated by C₂N's periodic porous structure with negatively charged “holes,” where the basic residues—such as lysine—can form stable interactions, thus functioning as “anchor points” in confining the protein displacement. It is suggested that the mild, immobilized protein attraction and biofriendly aspects of C₂N would make it a prospective candidate in bio‐ and medical‐related applications.