Given the inherent complexity of natural medicines, finding a straightforward and efficient method for identifying active ingredients remains a significant challenge, yet it is of paramount importance. Influenza virus neuraminidase (NA), a primary target for anti-influenza drug development, plays a crucial role in the infection process, making it essential to develop rapid and facile methods for screening NA inhibitors. Herein, we developed a novel and efficient analytical technique for the identification of NA inhibitors from complex herbal medicines by integrating dual sensing with affinity chromatography. This approach simplifies the experimental process and highlights the benefits of being quicker, more sensitive, and cost-effective. Regarding the biosensing section, the innovative concept of a 4-methylumbelliferyl-N-acetylneuraminic acid-NA-based fluorescence paper sensor strategy enables the rapid detection of NA inhibitors in complex herbal samples. In affinity chromatography, bioactive compounds were precisely captured, separated, and identified. The efficacy and reliability of the developed method were confirmed using both negative and positive controls. Then, the method was applied to screen for NA inhibitors in 20 different herbal medicines. The results revealed that Bupleurum chinense DC. exhibited the most pronounced inhibitory effect on NA. Subsequent analysis utilizing affinity chromatography identified three bioactive compounds, namely saikosaponin a, saikosaponin d, and baicalin, as the active agents responsible for this inhibitory effect, with IC₅₀ values of 177.3 μM, 262.9 μM, and 241.4 μM, respectively. Molecular docking studies further indicated that these three bioactive compounds exhibit a strong binding affinity with NA. This research provides novel insights into the screening of enzyme inhibitors within herbal medicines.

2025-03-01·COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY

Comprehensive review of chickpea (Cicer arietinum): Nutritional significance, health benefits, techno‐functionalities, and food applications

Review

作者: Garay, Antonio ; Yang, Jun ; Xu, Yixiang ; Zhang, Xin ; Hong, Shan ; Henderson, Douglas ; Li, Yonghui ; Zhu, Yi ; Kumar, Nandan

Abstract:

Chickpeas (Cicer arietinum L.) are globally valued legume known for their affordability, nutritional significance, and health benefits. They are rich in protein, fiber, vitamins, and minerals such as iron, zinc, folate, and magnesium. This review comprehensively explores the chemical composition of chickpeas and their functional properties, focusing on macronutrients, micronutrients, phytochemicals, and antinutritional factors. It also delves into the potential health benefits of bioactive compounds and peptides derived from chickpeas, highlighting their roles in various physiological functions and applications. The exceptional technofunctional properties of chickpea proteins, including gel formation, texture enhancement, emulsification, and fat/water binding, make them ideal ingredients for diverse food products. Their versatility allows for use in various forms (isolates, concentrates, textured proteins), contributing to the development of a wide range of plant‐based foods, nutritional supplements, and gluten‐free options. While chickpeas contain some antinutrients like phytates, lectins, and enzyme inhibitors, effective processing methods can significantly reduce their potential negative effects. This review provides valuable insights, offering the novel contributions and an enhanced understanding it brings to the scientific community and food industry. By bridging compositional data with physiological implications, the review reinforces the pivotal role of chickpeas as a dietary component and enriches the existing scientific literature on this essential legume.

2025-03-01·COMPUTERS IN BIOLOGY AND MEDICINE

The role of weak interactions in evaluation of inhibitory potential of Indinavir as an HIV protease inhibitor and its comparison with innovative drug candidates

Article

作者: Sabaghian, Hanieh ; Yoosefian, Mehdi

Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of -13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir.

100 项与 TNCE-3 相关的药物交易

登录后查看更多信息