Noscapine

Currently, there is concern about food products to which new psychoactive substances (NPS) have been added illegally. However, rapid, high-sensitivity, and high-throughput screening methods for such harmful substances have not been reported yet. In this study, a high-throughput non-targeted screening strategy was developed based on UHPLC-Q/Orbitrap. First, optimized pretreatment methods for typical high-risk matrices were established. Second, an accurate, efficient, and scalable high resolution mass spectrometry database containing 206 NPS and related compounds was constructed. The fragmentation pathways of three different types of fentanyl-related compounds were then systematically investigated to enhance compound identification. Additionally, a non-targeted screening strategy was developed using warning ions derived from 24 fentanyl-related compounds, streamlining the identification of NPS. This strategy was applied to 100 food samples with possible illegal additives and demonstrated its effectiveness. In summary, this study provides robust technical support for regulatory authorities in combating the illegal addition of food products.

Lactoferrin (LTF), a multifunctional glycoprotein, plays a critical role in iron metabolism, host defense mechanisms, and the regulation of inflammatory pathways. It is widely present in various mammalian secretions, including saliva, tears, and nasal fluids, and exhibits potent antimicrobial, immunomodulatory, and neuroprotective properties. Emerging evidence suggests that LTF may be pivotal in mitigating neurodegenerative diseases (NDs) by modulating oxidative stress and neuroinflammation. This study investigates the interaction of LTF with Noscapine, a benzylisoquinoline alkaloid known for its therapeutic potential, including anticancer and neuroprotective effects. Fluorescence binding studies revealed a strong binding affinity between LTF and Noscapine with a binding constant (K) of 0.1 × 10⁵ M^-1. Circular dichroism (CD) spectroscopy revealed subtle changes in LTF's secondary structure and a strong binding affinity between LTF and Noscapine, indicative of specific molecular interactions and conformational adjustments. Additionally, in silico studies were performed to complement the experimental findings. Molecular docking studies identified potential binding sites and highlighted key interactions stabilizing the LTF-Noscapine complex. Molecular dynamic (MD) simulation studies demonstrated that structural compactness is well preserved with only minimal structural alterations observed in the protein upon binding of Noscapine. Together, these results provide comprehensive insights into the molecular basis of LTF-Noscapine interaction, with potential implications for therapeutic applications in NDs. This study lays the groundwork for further exploration of Noscapine's potential in combating NDs and other biomedical challenges.