Antimicrobial peptides (AMPs) with dual intrinsic antibacterial and antioxidative functions have emerged as promising choice to cure infected wound. However, the most widely applied approach to endow AMPs with antioxidative function is to combine with antioxidative moieties, which may affect the spatial structure and physiological stability of AMPs. Herein, a new type of AMPs with inherent desired stability, antibacterial activity, and reactive oxygen species (ROS) scavenging is developed to effectively heal the infected wound. This formulation is in situ formed at wound site by tyrosinase‐triggered oxidation and self‐assembly of lyophilized antimicrobial peptide Trp‐Arg‐Trp‐Arg‐Trp‐Tyr, providing enhanced stability and a fourfold and sevenfold increasement in antibacterial efficiency against E. coli and S. aureus compared to peptide monomers. The antimicrobial peptide is first oxidized and then assembled into nanoparticles. The melanin‐like structure has been demonstrated with efficient antioxidant properties, and the experimental data show that peptide nanoparticles to scavenge superoxide radicals, hydroxyl radicals, and H2O2. In vivo experiments confirmed that peptide nanoparticles effectively heal infected wounds and obviously reduce ROS. Overall, the research provides a new approach to formulating antimicrobial peptides to treat wound with high healing efficiency.

In Situ Enzyme‐Induced Self‐Assembly of Antimicrobial‐Antioxidative Peptides to Promote Wound Healing

The flexible and controlled synthesis of metal-organic framework (MOF)-derived hybrid nanostructures is of great significance in fine tuning of their enrichment performance in large-scale and in-depth phosphoproteome analysis. Herein, a magnetic guanidyl-functionalized MOF hybrid coating with multiaffinity sites, denoted as Fe3O4@G-ZIF-8, was fast fabricated via a one-pot epitaxial growth strategy for the first time and applied for selective and highly efficient enrichment of global phosphopeptides. The intrinsic unsaturated metal sites of ZIF-8 endow the surface-mounted MOF coatings with immobilized metal ion affinity chromatography interaction with multiphosphorylated peptides. The oriented anchoring of bifunctional guanidineacetic acid on the magnetic MOF nanospheres provides additional affinity sites (guanidyl groups) for specific recognition of phosphopeptides by "salt bridge" interaction, as well as active site carboxyl groups for the coordination with the metal ions. The as-prepared Fe3O4@G-ZIF-8 exhibits large surface area (382.5 m2 g-1), good superparamagnetic property (41.6 emu g-1) and stability, and size-exclusion effect (1.73 nm), which can serve as a specific adsorbent for global phosphopeptide analysis with satisfactory selectivity, great detection sensitivity (1 fmol), and rapid magnetic separation. Moreover, the successful application of Fe3O4@G-ZIF-8 for selective capture of both multi- and mono-phosphopeptides from human saliva and serum demonstrated the great potential of magnetic surface-mounted MOF coatings in effective identification of low-abundance phosphopeptides by matrix-assisted laser desorption ionization time-of-flight mass spectrometry from complicated biological matrices.

Epitaxial Growth of Guanidyl-Functionalized Magnetic Metal-Organic Frameworks with Multiaffinity Sites for Selective Capture of Global Phosphopeptides.

Oxidative stress refers to the imbalance between the production of reactive oxygen species (ROS) and the endogenous antioxidant defense system. Its involvement in cell senescence, apoptosis, and series diseases has been demonstrated. Advances in carcinogenic research have revealed oxidative stress as a pivotal pathophysiological pathway in tumorigenesis and to be involved in lung cancer, glioma, hepatocellular carcinoma, leukemia, and so on. This review combs the effects of oxidative stress on tumorigenesis on each phase and cell fate determination, and three features are discussed. Oxidative stress takes part in the processes ranging from tumorigenesis to tumor death via series pathways and processes like mitochondrial stress, endoplasmic reticulum stress, and ferroptosis. It can affect cell fate by engaging in the complex relationships between senescence, death, and cancer. The influence of oxidative stress on tumorigenesis and progression is a multi-stage interlaced process that includes two aspects of promotion and inhibition, with mitochondria as the core of regulation. A deeper and more comprehensive understanding of the effects of oxidative stress on tumorigenesis is conducive to exploring more tumor therapies.

The Role of Oxidative Stress in Tumorigenesis and Progression

Si-rhodamine fluorescent probe for monitoring of hypochlorous acid in the brains of mice afflicted with neuroinflammation.

Uncovering the intrinsic interaction of different bioactive species, i.e., reactive oxygen species (ROS) and telomerase, is of great importance because they play interrelated and interdependent biological roles in living organisms. Nevertheless, exploration of the intracellular ROS/telomerase cross-talk by effective and noninvasive methods remains a great challenge, as it is difficult to simultaneously detect different types of biomolecules (i.e., active small molecules and proteins) in living cells. To address this issue, herein, we report, for the first time, a novel fluorescent nanoprobe for simultaneous determination and in situ imaging of telomerase activity and hydrogen peroxide (H2O2) in living cells. With the advantage of high sensitivity and good specificity, this newly fabricated nanoprobe was successfully applied to precisely visualize and monitor the changes in telomerase activity and H2O2 concentration in cancer cells. More significantly, by employing the nanoprobe as a one-step incubation tool, it is found that there is a cross-talk between H2O2 and telomerase activity in the drug-induced cancer cells' apoptosis process, which provides valuable information for gaining fundamental insights into the relationship between ROS and telomerase activity in cancer treatments. This work affords a promising method for revealing the relevant regulatory mechanisms and roles of ROS and telomerase activity in the occurrence, evolvement, and treatment of diseases.

Uncovering the Interaction between Intracellular Telomerase Activity and Hydrogen Peroxide during Cancer Cell Apoptosis Utilizing a Dual-Color Fluorescent Nanoprobe.

Revealing the relationship between reactive oxygen species (ROS) and levels of protein phosphorylation is of great significance for understanding the pathogenesis of diseases. Although mass spectrometry is used as a classical method for protein phosphorylation analysis, there are still some challenges to realize in vivo protein phosphorylation recognition. Herein, we designed and prepared an metal-organic framework (MOF)-based fluorescent nanoprobe with Zr(IV) and boronate ester as an active center, which achieved simultaneous recognition of ROS and phosphorylation sites. The ROS unit was constructed by 1,8-naphthalimide and boronate ester as a fluorophore and a recognition group, respectively. The specific interaction between Zr(IV) and a phosphate group was used to realize fluorescence imaging of phosphorylation sites. Using the advantages of two-photon property of the ROS recognition unit, the nanoprobe can effectively reduce the background fluorescence and thus improve the imaging sensitivity. Finally, the MOF-based nanoprobe was successfully applied to reveal the relationship between ROS and levels of phosphorylation in pneumonia mice, which illustrated that the ROS and phosphorylation levels in the process of pulmonary inflammation were obviously higher than those of the normal mice. This work provides feasible fluorescence tools that have important significance for revealing pathogenesis of diseases.

Elucidating the Relationship between ROS and Protein Phosphorylation through In Situ Fluorescence Imaging in the Pneumonia Mice.

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Elucidating the Relationship between ROS and Protein Phosphorylation through In Situ Fluorescence Imaging in the Pneumonia Mice.