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                    <title><![CDATA[Current Enzyme Inhibition (Volume 22 - Issue 1)]]></title>

                    <link>https://www.benthamscience.com/journal/17</link>

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                    RSS Feed for Journals <![CDATA[Current Enzyme Inhibition]]> | BenthamScience

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                    <pubDate>2026-03-03</pubDate>

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                    <title><![CDATA[Current Enzyme Inhibition (Volume 22 - Issue 1)]]></title>

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                    <link>https://www.benthamscience.com/journal/17</link>

                    </image><item><title><![CDATA[Preface]]></title><link>https://www.benthamscience.com/article/151520</link><pubDate>2026-03-03</pubDate><description><![CDATA[]]></description> </item><item><title><![CDATA[Advances in the Production of Recombinant Protease through Expression Systems: An Updated Review]]></title><link>https://www.benthamscience.com/article/148430</link><pubDate>2026-03-03</pubDate><description><![CDATA[Enzymes are proteins that act as biocatalysts and have been revolutionized in several fields and industries owing to their unique properties. Proteases are enzymes that hydrolyze peptide bonds in proteins. They are widely employed in the food, biotechnology, and pharmaceutical industries. As the demand for proteases increases, there is a growing focus on enhancing the expression and synthesis of protease enzymes in microorganisms using recombinant DNA technology, which has attracted attention due to its high potential in biotechnology. Several expression systems, such as <i>Bacillus, E. coli</i>, and <i>Saccharomyces cerevisiae</i>, are commonly employed for the synthesis of proteases. The accurate selection of an expression system for a microorganism depends greatly on the protease in terms of functional modifications and activity. However, the native protease host does not show increased expression. As a result, the production of recombinant proteases has emerged as a crucial target that provides a high yield of protease and is cost-effective. Despite this advancement, there are still some challenges, such as the specificity and stability of the expression systems. This review presents an overview of the primary factors that enhance protein expression, as well as several strategies that increase the production of recombinant proteases, such as improving signal peptidases, promoter regions, and fermentation conditions. The applications of protease enzymes are also discussed, with the aim of presenting diverse sources and approaches for producing recombinant proteases using various expression systems. Furthermore, protease production from expression systems is still evolving, offering a wide range of applications in diverse industries.]]></description> </item><item><title><![CDATA[Advances in Liposome Technology: An Intensive Review of Formulation, Therapeutic Applications, and Challenges]]></title><link>https://www.benthamscience.com/article/149213</link><pubDate>2026-03-03</pubDate><description><![CDATA[<p>Introduction: Liposomes are versatile drug delivery vehicles due to their nanoscale lipid bilayer vesicles, capable of encapsulating both hydrophilic and hydrophobic substances. They have shown promise in vaccine development, gene therapy, cancer treatment, and targeted drug delivery. However, their clinical applicability is limited due to factors like drug stability, manufacturing constraints, regulatory challenges, and immune responses. This study explores liposome formulations by focusing on enhanced stability, robustness, and drug-loading efficiency. It also discusses therapeutic implementation challenges. </p> <p> Methods: A systematic literature review was conducted using specific keywords and Boolean operators across databases, such as Web of Science, PubMed, and Scopus. Non-peer-reviewed articles, conference abstracts, and studies with poor methodology were excluded. </p> <p> Results: This review highlights advances in liposome formulation that boost therapeutic performance, enhance stability, and improve drug loading. Despite their promise, clinical application depends on overcoming issues like manufacturing complexity, regulatory constraints, and immune reaction limitations. </p> <p> Discussion: Liposomes enable efficient encapsulation and targeted delivery for both hydrophilic and hydrophobic drugs, enhancing therapeutic efficacy. Their biocompatibility makes them effective in cancer therapy, vaccine transport, and gene delivery. Nevertheless, further research is needed to improve production processes and ensure long-term safety for regulatory approval and commercial scalability. </p> <p> Conclusion: Liposomes hold strong potential for medical use and drug delivery. To achieve broader clinical adoption, challenges in formulation and regulation must be addressed. This review highlights recent innovations and strategies to optimize liposome-based therapeutics.</p>]]></description> </item><item><title><![CDATA[Development of a Robust QSAR Model to Predict the Affinity of N-Bridged Bicyclic Sulfonamide, Pyrazole/Sulfonamide Based Dihydroquinoline and Sulfonamide –Pyrazolopiperidine &#947;-secretase Inhibitors]]></title><link>https://www.benthamscience.com/article/148098</link><pubDate>2026-03-03</pubDate><description><![CDATA[<p>Introduction: &#947;-secretase has been a primary target for the creation of therapies that alter the course of Alzheimer's disease. Compounds inhibiting &#947;-secretase, targeting PS-1, are potential therapeutic agents for Alzheimer’s disease. </p> <p> Methods: The model was generated with the help of linear and non-linear regression analysis methods. The analysis helped to ascertain the role of log P (whole molecule), no. of H-bond (whole molecule), Kier ChiV3(cluster indices), and Kier Chi6 (ring index) in determining the activity of &#947; secretase inhibitors. In addition to QSAR modelling, Lipinski’s rule of five was also employed to check the pharmacokinetic profile of &#947;-secretase inhibitors. </p> <p> Results: Significant statistical values of the designed models were obtained with the help of MLR, PLS, and FFNN analysis and the relevant descriptors. </p> <p> Discussion: QSAR (Quantitative Structure-Activity Relationship) models generated (both MLR and PLS) were robust with statistically significant s, F, r, r2 and r2CV values. This study conducts QSAR analysis using linear regression analysis and non-linear regression analysis on a data set of 53 compounds acting as &#947;-secretase inhibitors. </p> <p> Conclusion: None of the compounds violated Lipinski’s rule of five, indicating that the &#947;-secretase inhibitors reported here have sound pharmacokinetic profiles and can be considered as potential drug candidates for Alzheimer’s disease.</p>]]></description> </item><item><title><![CDATA[Neuroprotective Potential of <i>Oroxylum indicum</i> Seeds in Antioxidant Activity, Enzyme Inhibition and Cognitive Improvement for Alzheimer's Disease]]></title><link>https://www.benthamscience.com/article/149031</link><pubDate>2026-03-03</pubDate><description><![CDATA[<p>Introduction: Alzheimer’s disease (AD) is a debilitating neurodegenerative disorder marked by progressive memory loss and cognitive decline. Oxidative stress and cholinergic dysfunction are central to its pathology. Natural products with antioxidant and cholinesterase-inhibitory activities are gaining attention as potential therapeutic agents. This study explores the neuroprotective potential of Oroxylum indicum seed extract. </p> <p> Methods: Methanolic extraction of <i>Oroxylum indicum</i> seeds was followed by phytochemical screening. Bioactive compounds were isolated via column chromatography and characterized using FTIR, NMR, and mass spectrometry. Antioxidant potential was assessed through DPPH, nitric oxide (NO), and hydroxyl radical scavenging assays. <i>In vitro</i> acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibition assays were conducted, and molecular docking was performed to evaluate binding affinities. </p> <p> Results: Baicalein and chrysin were identified as major constituents. Both compounds showed potent antioxidant activity: baicalein (IC<sub>50</sub> = 49.79 ± 0.033 μg/mL for DPPH, 30.48 ± 0.092 μg/mL for NO, and 48.56 ± 0.10 μg/mL for •OH) and chrysin (IC<sub>50</sub> = 66.24 ± 0.032, 38.73 ± 0.030, and 52.18 ± 0.12 μg/mL, respectively). They also exhibited strong enzyme inhibition: baicalein (AChE: 40.73 μg/mL, BChE: 35.76 μg/mL) and chrysin (AChE: 52.74 μg/mL, BChE: 31.56 μg/mL). Docking studies supported these findings, showing strong binding affinities to the active sites of AChE and BChE. </p> <p> Discussion: The strong free radical scavenging and cholinesterase-inhibitory effects of baicalein and chrysin highlight their potential to mitigate oxidative stress and cholinergic dysfunction in AD. </p> <p> Conclusion: <i>Oroxylum indicum</i> seed-derived baicalein and chrysin exhibit promising neuroprotective properties and represent potential candidates for the development of AD therapeutics.</p>]]></description> </item><item><title><![CDATA[Evaluating the Antioxidant Activity of Four Iranian <i>Euphorbia</i> Species and Molecular Docking Analysis of Effective Compounds]]></title><link>https://www.benthamscience.com/article/149177</link><pubDate>2026-03-03</pubDate><description><![CDATA[<p>Introduction: Medicinal plants are a rich source of natural antioxidants and play an important role in preventing oxidative stress-related diseases. This study aimed to evaluate the antioxidant activity of four Iranian <i>Euphorbia</i> species (<i>E. malleata, E. gypsicola, E. caspica</i>, and <i>E. sylvicola</i>). </p> <p> Methods: The antioxidant activity of methanolic extracts from these species was evaluated using the DPPH assay. The most potent species was further subjected to fractionation, and each fraction was assessed using the same method. Subsequently, the antioxidant activity of compounds isolated from the effective fraction was evaluated using molecular docking against the MPO enzyme. </p> <p> Results: <i>E. malleata</i> exhibited the strongest DPPH radical scavenging activity among the four species. Its ethyl acetate fraction demonstrated the highest scavenging activity with an IC<sub>50</sub> value of 2.65 μg/ml. Among the ethyl acetate fraction compounds, methyl gallate showed the most favorable docking score (-4.97 kcal/mol) and formed multiple hydrogen bonds with key MPO residues. </p> <p> Discussion: The remarkable free radical scavenging activity of E. malleata ethyl acetate fraction is closely associated with the presence of flavonoids and phenolic compounds. Molecular docking indicated that methyl gallate forms a stable complex with the MPO receptor, suggesting its potential as a promising MPO inhibitor. </p> <p> Conclusion: The ethyl acetate fraction of <i>E. malleata</i> and its compounds indicated significant antioxidant activity and the capacity to inhibit the MPO enzyme. The findings highlight the therapeutic potential of the E. malleata species, making it an attractive candidate for further investigation in pharmaceutical applications, particularly for the development of therapies targeting inflammatory and oxidative stress-related illnesses.</p>]]></description> </item><item><title><![CDATA[Design, Synthesis, and Biological Evaluation of Triazine-4-Thiazolidinone Hybrid Molecules as Modulator of Breast Cancer]]></title><link>https://www.benthamscience.com/article/146825</link><pubDate>2026-03-03</pubDate><description><![CDATA[<p>Introduction/Objective: Breast cancer is the most prevalent cancer among women globally, characterized by the uncontrolled growth of breast cells, and remains a leading cause of cancerrelated morbidity and mortality. It can occur in both men and women, though it is significantly rarer in men. The multifactorial nature of breast cancer involves genetic mutations, hormonal influences, and complex cellular signalling pathways. The disease is typically classified into different subtypes based on hormone receptor status, which influences treatment decisions. Early detection through regular screening, such as mammograms, and awareness of symptoms significantly improve prognosis. Treatment options vary based on the stage and type of breast cancer and may include surgery, radiation therapy, chemotherapy, hormone therapy, and targeted therapy. We aimed to design novel compounds based on reported active pharmacophoric features and validate them through molecular modelling. These designed compounds were then synthesized and characterized. Finally, a biological evaluation of the synthesized compounds was performed to assess their efficacy. </p> <p> Methods: Thirty compounds were designed based on a literature survey. Out of these compounds, twelve compounds were found good on the docking studies, and these twelve new derivatives (RD 01-12) were synthesized and subjected to <i>in silico, in vitro</i> (EGFR assay), and ADMET profiling to identify the most potent compound. </p> <p> Results: All 12 compounds were synthesised and characterised. Out of 12 compounds, RD-09 emerged as the most potent enzymatic assay with an IC<sub>50</sub> value of 1.21 ± 0.03 μM, confirmed by docking studies; it possessed a docking score of -7.302 against the EGFR receptor. These compounds were further characterized using IR, <sup>1</sup>H NMR, and mass spectrometry. </p> <p> Conclusion: Based on pharmacophoric features, twelve triazine-4-thiazolidinone derivatives (RD 01- 12) were designed, synthesized, and evaluated for their potential as EGFR-2 inhibitors, specifically targeting triple-negative breast cancer (TNBC). Among 12 synthesised compounds, compound RD- 09 demonstrated the most significant activity with an IC50 value of 1.21 ± 0.03 μM. Docking studies further supported its binding interaction with the catalytic domain of the EGFR receptor. The combined results from <i>in vitro, in silico</i>, and ADMET profiling suggest that RD-09 holds promise as a leading compound for further development in the treatment of TNBC.</p>]]></description> </item></channel></rss>