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The physiological inhibitors of soluble epoxide hydrolase (sEH) have significant efficacy in the treatment of hypertension, inflammation, cardiovascular disease and diabetes. In this study, a Hypogen pharmacophore was developed using Atlantic cod peptide and was used to screen for bioactive peptides with tryptophan and sEH inhibitory activity by molecular docking. Bioactive peptide sequences were prepared by solid-phase synthesis, and their in vitro sEH inhibitory activity was determined by high performance liquid chromatography (HPLC). The results showed that the tetrapeptide (PLLW) selected by the optimal pharmacophore model had the best Fit value (9.053) and LibDock score (147.807), and its half-maximal inhibitory concentration (IC50) was 506.66 μmol/L. The molecular docking results showed that PLLW competed with physiological substrates to bind to the active site of sEH through hydrogen bonding and hydrophobic interactions. This study provides a new idea for the screening and mechanistic study of sEH inhibitors in foodborne mixed systems, and also provides a suitable model for the development of sEH inhibitor products.

Background: In this systematic review and meta‐analysis, we aimed to validate the predictive role of atrial fibrillation (AF) termination in long‐term arrhythmia recurrence. Method: Our search encompassed databases including MEDLINE, EMBASE, PubMed, and the Cochrane Library up to August 1, 2021. Three independent reviewers conducted screening and data extraction. The data included ablation strategy, recurrence mode, AF termination mode, numbers of patients, and recurrence cases in the termination and nontermination groups. The primary endpoint was the recurrence of atrial arrhythmia at long‐term follow‐up (≥ 12 months). Results: Our analysis included 22 publications, with 11 prospective studies being eligible for further meta‐analysis. Among these, 14 studies reported significantly lower rates of arrhythmia recurrence in the AF termination group compared to the nontermination group. Among seven studies involving 1114 patients that examined single procedure outcomes, the pooled estimated effect was RR 0.78 (95% CI 0.68–1.90) with an I2 value of 57%. Subgroup analysis focusing on termination mode as sinus rhythm yielded a pooled estimated effect of RR 0.74 (95% CI 0.59–0.92) with an I2 value of 47%. Additionally, analysis of seven studies involving 1433 patients for repeat procedures demonstrated a significant preference for the AF termination group (RR 0.83, 95% CI 0.71–0.97, I2 = 84%). Subgroup analysis indicated reduced heterogeneity when the termination mode was sinus rhythm (RR 0.68, 95% CI 0.51–0.90, I2 = 57%). Conclusion: Our study establishes that AF termination serves as an effective predictor for the success of persistent AF ablation procedures. This finding holds potential implications for clinical practice and contributes to our understanding of long‐term arrhythmia recurrence in the context of AF termination. [ABSTRACT FROM AUTHOR]

Protein lattices that shift the structure and shape anisotropy in response to environmental cues are closely coupled to potential functionality. However, to design and construct shape‐anisotropic protein arrays from the same building blocks in response to different external stimuli remains challenging. Here, by a combination of the multiple, symmetric interaction sites on the outer surface of protein nanocages and the tunable features of phenylalanine‐phenylalanine interactions, a protein engineering approach is reported to construct a variety of superstructures with shape anisotropy, including 3D cubic, 2D hexagonal layered, and 1D rod‐like crystalline protein nanocage arrays by using one single protein building block. Notably, the assembly of these crystalline protein arrays is reversible, which can be tuned by external stimuli (pH and ionic strength). The anisotropic morphologies of the fabricated macroscopic crystals can be correlated with the Å‐to‐nm scale protein arrangement details by crystallographic elucidation. These results enhance the understanding of the freedom offered by an object's symmetry and inter‐object π−π stacking interactions for protein building blocks to assemble into direction‐ and shape‐anisotropic biomaterials. [ABSTRACT FROM AUTHOR]