Scientia Pharmaceutica

Leaves of plants in the Zingiberaceae family are traditionally consumed as vegetables and used as herbal ingredients. However, the phytochemical composition and bioactive potential of Zingiberaceae leaves remain less investigated than those of rhizomes. This study evaluated the phytochemical composition, amino acid profiles, and antioxidant activities of leaves from four Zingiberaceae species, including Boesenbergia rotunda, Kaempferia marginata, Zingiber montanum, and Zingiber officinale. Total phenolics (TPC), total flavonoids (TFC), vitamin C, phenolic acids, flavonoids, and amino acids in the leaves were determined using HPLC and LC–MS/MS and associated with antioxidant activities (DPPH and FRAP assays). Significant differences among species were observed (p < 0.05). Z. montanum leaves exhibited the highest TPC (7.04 mg GAE/g DW), whereas Z. officinale leaves showed the highest vitamin C content (227.42 mg/100 g). The highest total phenolic acids were detected in K. marginata leaves (4830.36 µg/g DW), with caffeic acid as the dominant compound. In contrast, Z. officinale leaves contained the highest flavonoid content (16,255.10 µg/g DW), particularly rutin (15,123.09 µg/g DW). Amino acid analysis revealed that K. marginata leaves had the highest total amino acids (114.41 µg/g DW). Multivariate analyses demonstrated distinct phytochemical profiles among species, highlighting the chemical diversity and bioactive potential of Zingiberaceae leaves.

ICH Q1B sets a standardized photostability test for new drug substances and products, with a confirmatory exposure of at least 1.2 × 10⁶ lux hours of visible light and 200 W·h/m² of near-ultraviolet energy. It was finalized in 1996, when only two therapeutic monoclonal antibodies had been approved in the United States; the FDA approved its 100th in 2021. This review asks whether Q1B remains fit for purpose for this product class. We distinguish lack of real-world representativeness from lack of fitness for Q1B’s stated purpose of informing handling, packaging, and labeling. The confirmatory exposure greatly exceeds, and differs spectrally from manufacturing and clinical light, but that is by design. The weaknesses that matter are interpretive: little biologics-specific guidance on justifying alternative exposures, no recognition of excipient- and metal-mediated photochemistry that can vary between batches, and no antibody-specific direction on endpoints such as aggregation, charge variants, site-specific oxidation, and Fc receptor binding. The review covers antibody photochemistry, including IgG2- and IgG4-specific considerations; a quantitative comparison of test and real-world light; an orthogonal analytical toolbox; and formulation, container, and infusion-set mitigations. It also assesses the ICH Q1 draft guideline (Step 2b, April 2025), which recognizes that ambient light lies mainly above 400 nm and adds in-use stability, but retains the 1.2 × 10⁶ lux hour confirmatory condition and does not address formulation-mediated photochemistry. A two-track framework is proposed that keeps the harmonized exposure for hazard identification and adds exposure-representative testing for risk assessment.

Antimicrobial peptides (AMPs) interact with bacterial membranes through mechanisms influenced by both peptide properties and membrane lipid composition. This study investigated the interactions of crotalicidin (Ctn) and its C-terminal fragment (Ctn[15–34]) with model membranes mimicking Escherichia coli, Klebsiella pneumoniae, and Staphylococcus aureus using Fourier-transform infrared spectroscopy. Both peptides showed membrane-dependent conformational changes, with the extent of α-helical formation varying with lipid composition. Ctn showed the greatest increase in α-helical content in the S. aureus model, whereas Ctn[15–34] exhibited lower α-helical propensity in the Gram-negative membrane models. We assessed membrane thermotropic behavior by monitoring temperature-dependent changes in the CH₂ and C=O stretching bands. Ctn markedly increased the main phase transition temperature (T_m) of the E. coli and K. pneumoniae membrane models, while its effect on the S. aureus model was limited. Similarly, Ctn[15–34] increased T_m in the E. coli model, with a smaller increase observed in K. pneumoniae. In contrast, a slight decrease in T_m was observed in the S. aureus model. Analysis of individual lipids revealed that dimirystoylphosphatidylglycerol (DMPG) was the most strongly affected, with Ctn[15–34] decreasing its Tm by up to 6.59 °C. Overall, these findings suggest that Ctn and Ctn[15–34] interactions with bacterial membrane models are influenced by peptide physicochemical properties and membrane lipid composition, highlighting that α-helical formation alone does not account for the observed membrane responses.