Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

In Vitro, In Silico and Structure-Activity Relationship Evaluation of 3-Amino-thiophene-2-carbohydrazides as Lactoperoxidase Inhibitors.

Archiv der Pharmazie·2026
Same author

Integrated machine learning and molecular dynamics-driven multi-target virtual screening of FDA-approved drugs for drug repurposing in breast cancer.

In silico pharmacology·2026
Same author

Decoding PI3K isoform selectivity through an ensemble-based framework integrating correlated motions, allosteric networks, and hydration thermodynamics.

Journal of biomolecular structure & dynamics·2026
Same author

Thermodynamic Preference of Fe<sup>2+</sup> for a C-Terminal Coordination Site in Human Frataxin Revealed by Multiscale Simulations.

Journal of chemical information and modeling·2026
Same author

Schiff Base Derivatives as Carbonic Anhydrases and Cholinesterases Inhibitors: Molecular Docking and Anticancer Studies.

Journal of biochemical and molecular toxicology·2026
Same author

Structure-Based Virtual Screening of Plant-Derived Flavonoids as Putative GLUT9 Binders with Antioxidant Properties.

Molecules (Basel, Switzerland)·2026

Related Experiment Video

Updated: Jun 26, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Sulfonamide Derivatives as Competitive Lactoperoxidase Inhibitors Through Integrated Experimental and Multi-Level

Kevser Kübra Kırboğa1, Şükran Acar1, Zeynep Köksal2,3

  • 1Faculty of Engineering, Department of Bioengineering, Bilecik Şeyh Edebali University, Bilecik, Türkiye.

Journal of Biochemical and Molecular Toxicology
|June 25, 2026
PubMed
Summary

Three sulfonamide derivatives were tested as inhibitors of lactoperoxidase (LPO), an enzyme crucial for innate immunity. Naphthalene-2-sulfonamide demonstrated the strongest inhibitory effect, showing promise for future drug development.

Keywords:
DFTenzyme kineticsheme enzyme inhibitionlactoperoxidasestructure‐based drug designsulfonamide

More Related Videos

Measuring Lactase Enzymatic Activity in the Teaching Lab
04:41

Measuring Lactase Enzymatic Activity in the Teaching Lab

Published on: August 6, 2018

Related Experiment Videos

Last Updated: Jun 26, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Measuring Lactase Enzymatic Activity in the Teaching Lab
04:41

Measuring Lactase Enzymatic Activity in the Teaching Lab

Published on: August 6, 2018

Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Lactoperoxidase (LPO) is a key enzyme in mammalian innate immunity, involved in antimicrobial defense.
  • Selective inhibition of LPO is of interest for mechanistic studies and therapeutic applications, especially concerning oxidative stress.

Purpose of the Study:

  • To evaluate three sulfonamide derivatives (Naphthalene-2-SA, 2,5-DCTSA, 6-APSA) as inhibitors of bovine LPO.
  • To combine experimental data with multi-level computational approaches to understand sulfonamide-LPO interactions.

Main Methods:

  • Purification of bovine LPO from skimmed milk using affinity chromatography.
  • In vitro kinetic assays to determine inhibitory activity (IC50, Ki) and mechanism.
  • Computational analyses including molecular docking, molecular dynamics simulations, MM-GBSA, and DFT calculations.

Main Results:

  • All three sulfonamides acted as competitive inhibitors of LPO.
  • Naphthalene-2-SA exhibited the highest potency (IC50 = 0.69 µM, Ki = 0.50 µM).
  • Computational methods consistently identified Naphthalene-2-SA as the top-ranked inhibitor, aligning with experimental findings and DFT reactivity descriptors.

Conclusions:

  • The study provides mechanistic insights into sulfonamide interactions with LPO.
  • Naphthalene-2-SA is identified as a promising lead compound for developing novel LPO inhibitors.