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Optimizing the zymogram of exogenous proteases in broiler diets by in vitro simulated gastrointestinal digestion and response surface methodology.
Sci Rep
February 2025
Department of Animal Nutrition, Hunan Institute of Animal Husbandry and Veterinary Medicine, Changsha, 410125, China.
Low protein digestibility causes intestinal flora imbalance, wet litter, and nitrogen pollution. The present study aimed to explore the optimal zymogram of exogenous acid protease (ACP), neutral protease (NEP), alkaline protease (ALP), and keratinase (KEA) in corn-soybean based diets for broilers. The hydrolysis performances of the four monocomponent proteases were presented by enzymatic hydrolysate gross energy (EHGE) and improved dry matter digestibility (IDMD), which were tested via the in vitro simulated digestion method.
View Article and Find Full Text PDFThe catalytic action of enzymes exposed to charged substrates outperforms the activity exerted on their neutral counterparts.
Biochem Biophys Res Commun
March 2025
Department of Pharmacy and Biotechnology, Viale Risorgimento 4, 40136, Bologna, Italy; CSGI, University of Firenze, Via della Lastruccia 3, 50019, Sesto Fiorentino, FI, Italy. Electronic address:
Enzymes perform their catalytic action according to mechanisms featuring exquisite specificity, up to the selection of substrate conformers. However, regardless of this high specificity enzymes are able to deal with a repertoire of substrates, whose conversion into reaction products can occur with markedly different rates. Among the factors affecting the velocity of enzyme-catalyzed reactions, the presence in the substrate of an electrostatic charge could be of importance.
View Article and Find Full Text PDFSynthesis and biological evaluation of new dual APN/NEP inhibitors as potent analgesics.
Bioorg Chem
March 2025
School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, China. Electronic address:
An alternative approach for the management of acute and chronic pains involves prolonging the half-life of endogenous opiates, such as enkephalins that are released in response to nociceptive stimuli. This can be achieved through the inhibition of enzymatic pathways responsible for the hydrolysis of these peptides, particularly targeting Aminopeptidase N (APN) and Neutral Endopeptidase (NEP). In this study, we designed and synthesized a series of dual enkephalinase inhibitors (DENKIs) targeting both APN and NEP as novel analgesic treatments.
View Article and Find Full Text PDFDissecting the Binding Affinity of Anti-SARS-CoV-2 Compounds to Human Transmembrane Protease, Serine 2: A Computational Study.
Int J Mol Sci
January 2025
State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan and School of Life Sciences, Yunnan University, Kunming 650091, China.
The human transmembrane protease, serine 2 (TMPRSS2), essential for SARS-CoV-2 entry, is a key antiviral target. Here, we computationally profiled the TMPRSS2-binding affinities of 15 antiviral compounds. Molecular dynamics (MD) simulations for the docked complexes revealed that three compounds exited the substrate-binding cavity (SBC), suggesting noncompetitive inhibition.
View Article and Find Full Text PDFPositively charged cytoplasmic residues in corin prevent signal peptidase cleavage and endoplasmic reticulum retention.
Commun Biol
January 2025
Cyrus Tang Hematology Center, Collaborative Innovation Center of Hematology, State Key Laboratory of Radiation Medicine and Prevention, Suzhou Medical College, Soochow University, Suzhou, 215123, China.
Positively charged residues are commonly located near the cytoplasm-membrane interface, which is known as the positive-inside rule in membrane topology. The mechanism underlying the function of these charged residues remains poorly understood. Herein, we studied the function of cytoplasmic residues in corin, a type II transmembrane serine protease in cardiovascular biology.
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