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H. Alqhtani

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Open access Jul 2026

Identification of reproductive and molecular biomarkers associated with clinical metritis in dromedary camels (Camelus dromedarius)

Background Metritis is a major cause of infertility, contributing to repeat breeding, early embryonic loss, fetal mortality, and abortion. Methods This study investigated alterations in metabolic, hormonal, oxidative, immunological, and molecular markers associated with metritis susceptibility in dromedary camels (Camelus dromedarius). A total of 100 non-lactating multiparous females (87 healthy and 13 metritic) were examined. Blood samples were collected and analyzed to evaluate hematobiochemical parameters, inflammatory and antioxidant markers, and single nucleotide polymorphisms (SNPs) in selected immune- and antioxidant-related genes. Results Metritic animals exhibited fever and abnormal uterine discharge. Gene expression analysis showed significant upregulation of CARD9, SIGLEC1, VSIG4, BTRC, SLC2A3, ACOD1, and PFKFB3, alongside downregulation of CPT1A, ATF4, GADD45B, SLC7A11, and PRDX3. Sequencing identified 19 SNPs, with significant differences in genotype distribution between groups, and discriminant analysis achieved complete classification accuracy. Hematological findings included normocytic normochromic anemia, leukocytosis, neutrophilia, lymphopenia, and monocytosis. Biochemically, metritic camels showed hypoglycemia and decreased levels of estrogen, progesterone, FSH, LH, T4, calcium, and antioxidant markers (GSH, CAT, and TAC), while NEFA, BHBA, cortisol, MDA, and pro-inflammatory cytokines (IL1α, IL1β, IL6, IL10, and TNFα) were significantly elevated. Conclusion Overall, clinical metritis in dromedary camels was associated with significant hematological, metabolic, hormonal, oxidative, immunological, and genetic alterations. These findings identify a panel of reproductive and molecular biomarkers that may serve as promising candidate biomarkers associated with clinical metritis. However, given the observational nature of the study and the relatively small number of metritic she-camels, these findings should be interpreted with caution and require validation in larger, independent camel populations before their diagnostic, prognostic, or breeding applications can be established.

H. Alqhtani, Ahmed Elsayed, Tahani M. I. Al-Hazani et al. · Frontiers in Veterinary Scie... · 0 citations

Aug 2026

Structure-guided delineation of umbelliferyl phosphate-based disruptors of the c-Myb-CBP/p300 KIX protein-protein interaction.

The interaction between c-Myb and the CBP/p300 KIX domain is a critical transcriptional regulatory event and an attractive target for the development of candidate disruptors of the recombinant c-Myb-KIX interaction. In this study, we used an integrated computational and experimental strategy to identify new small molecules capable of disrupting this protein-protein interaction. A focused Umbelliferyl phosphate scaffold library was subjected to stepwise virtual screening via drug-likeness assessment and docking to the c-Myb-binding region of the KIX domain and short molecular dynamics refinement. Selected compounds were then evaluated by 500 ns molecular dynamics simulations, MM/PBSA analysis, free energy landscape (FEL) mapping, and finally by microscale thermophoresis (MST) assay. Computational analyses showed that stable ligand binding did not necessarily translate into disruption of the c-Myb-KIX interface, allowing separation of compounds that stabilized the complex from those predicted to weaken it. Consistent with this distinction, ΔΔGPPIanalysis identified only MUP and Naphthol AS-BI phosphate as protein-protein interaction-weakening ligands, with Naphthol AS-BI phosphate showing the strongest predicted disruptive effect (ΔΔGPPI=+3.25 kcal/mol), whereas DiFMUP and Naphthol AS-D phosphate were predicted to stabilize the complex. Among the tested molecules, Naphthol AS-BI phosphate showed the clearest disruption-like behavior in silico and was the most potent inhibitor in vitro, with an IC₅₀ of 18.9 ± 0.6 μM. Importantly, MUP emerged as the most promising umbelliferyl phosphate-derived hit, displaying measurable inhibitory activity (IC₅₀ = 33.5 ± 0.3 μM) comparable to the reference Naphthol AS-E phosphate (IC₅₀ = 31.2 ± 1.3 μM) and a more favorable predicted ADMET profile. Overall, this work identifies new chemical starting points for targeting the c-Myb-CBP/p300 KIX interaction and supports MUP as an attractive scaffold for further optimization.

Emadeldin M. Kamel, H. Rudayni, A. A. Allam et al. · Biophysical Chemistry · 0 citations