Related Experiment Video
Updated: Jan 9, 2026

Biochemical Measurement of Neonatal Hypoxia
Published on: August 24, 2011
Exploration, sequence optimization and inhibition mechanisms of xanthine oxidase inhibitory peptides from chicken
Jun Li1, Shiqin Lai1, Wen Hu1
1Guangdong Provincial Key Laboratory of Lingnan Specialty Food Science and Technology, Key Laboratory of Green Processing and Intelligent Manufacturing of Lingnan Specialty Food, Ministry of Agriculture and Rural Affairs, College of Light Industry and Food, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China.
Abstract:
Compared to conventional pharmacological therapies, xanthine oxidase (XO) inhibitory peptides offer a potentially safer approach for managing hyperuricemia. In this study, a good XO-inhibitory fraction was separated from chicken hemoglobin hydrolysate and 11 peptides were screened by in silico screening. Subsequent synthesis and activity validation revealed that three peptides, WPDNGFPGPQ, PPNSDIGWRV, and NGPAHW, significantly inhibited XO activity via non-competitive or mixed-type inhibition, with IC₅₀ values of 3.95, 4.85, and 6.39 mM, respectively. Molecular docking and dynamic simulations indicated that these peptides binded tightly to XO primarily through hydrogen bonding and hydrophobic interactions. Furthermore, optimization studies on WPDNGFPGPQ demonstrated that an optimal chain length is critical for effective XO inhibition, with the nonapeptide derivative (WPDNGFPGP) exhibiting the strongest activity. These findings suggest that chicken hemoglobin represents a promising natural source of bioactive peptides for the potential treatment of hyperuricemia.
More Related Videos
08:31Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
12:08Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Related Concept Videos
Enzyme Inhibition
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Anticholinesterase Agents: Poisoning and Treatment
Irreversible agents form a strong bond with the cholinesterase enzyme, making it inactive. The breakdown of the phosphorylated enzyme is...
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...