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Binding of omeprazole to protein targets identified by monoclonal antibodies
- Source :
- PLoS ONE, PLoS ONE, Vol 15, Iss 9, p e0239464 (2020)
- Publication Year :
- 2020
- Publisher :
- Public Library of Science, 2020.
-
Abstract
- Omeprazole is the most commonly used proton pump inhibitor (PPI), a class of medications whose therapeutic mechanism of action involves formation of a disulfide linkage to cysteine residues in the H+/K+ ATPase pump on gastric secretory cells. Covalent linkage between the sole sulfur group of omeprazole and selected cysteine residues of the pump protein results in inhibition of acid secretion in the stomach, an effect that ameliorates gastroesophageal reflux and peptic ulcer disease. PPIs, though useful for specific conditions when used transiently, are associated with diverse untoward effects when used long term. The mechanisms underlying these potential off-target effects remain unclear. PPIs may, in fact, interact with non-canonical target proteins (non-pump molecules) resulting in unexpected pathophysiological effects, but few studies describe off-target PPI binding. Here, we describe successful cloning of monoclonal antibodies against protein-bound omeprazole. We developed and used monoclonal antibodies to characterize the protein target range of omeprazole, stability of omeprazole-bound proteins, and the involvement of cysteines in binding of omeprazole to targets. We demonstrate that a wide range of diverse proteins are targeted by omeprazole. Protein complexes, detected by Western blotting, are resistant to heat, detergents, and reducing agents. Reaction of omeprazole occurs with cysteine-free proteins, is not fully inhibited by cysteine alkylation, occurs at neutral pH, and induces protein multimerization. At least two other clinically used PPIs, rabeprazole and tenatoprazole, are capable of binding to proteins in a similar fashion. We conclude that omeprazole binds to multiple proteins and is capable of forming highly stable complexes that are not dependent on disulfide linkages between the drug and protein targets. Further studies made possible by these antibodies may shed light on whether PPI-protein complexes underlie off-target untoward effects of chronic PPI use.
- Subjects :
- Serum Proteins
Disulfide Linkage
Physiology
Cancer Treatment
Plasma protein binding
Biochemistry
Antibodies, Monoclonal, Murine-Derived
Mice
0302 clinical medicine
Immune Physiology
Medicine and Health Sciences
Drug Interactions
030212 general & internal medicine
Amino Acids
Enzyme-Linked Immunoassays
Omeprazole
Mice, Inbred BALB C
Multidisciplinary
Immune System Proteins
Chemistry
Organic Compounds
Oncology
Reducing Agents
Physical Sciences
Medicine
medicine.symptom
Protein Binding
medicine.drug
Research Article
medicine.drug_class
Science
Immunology
Proton-pump inhibitor
Monoclonal antibody
Research and Analysis Methods
Antibodies
03 medical and health sciences
Antibody Therapy
medicine
Animals
Humans
Sulfur Containing Amino Acids
Cysteine
Binding site
Immunoassays
Pharmacology
Binding Sites
Organic Chemistry
Chemical Compounds
Biology and Life Sciences
Proteins
Proton Pump Inhibitors
Monoclonal Antibodies
Mice, Inbred C57BL
HEK293 Cells
Mechanism of action
Multiprotein Complexes
Immunologic Techniques
Clinical Immunology
Clinical Medicine
030217 neurology & neurosurgery
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 15
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....dec6116c96b57f5740372cabb6ba534b