Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen.
Abstract: Serum albumin, a protein naturally abundant in blood plasma, shows remarkable ligand binding properties of numerous endogenous and exogenous compounds. Most of serum albumin binding sites are able to interact with more than one class of ligands. Determining the protein-ligand interactions among mammalian serum albumins is essential for understanding the complexity of this transporter. We present three crystal structures of serum albumins in complexes with naproxen (NPS): bovine (BSA-NPS), equine (ESA-NPS), and leporine (LSA-NPS) determined to 2.58 Å (C2), 2.42 Å (P61), and 2.73 Å (P2₁2₁2₁) resolutions, respectively. A comparison of the structurally investigated complexes with the analogous complex of human serum albumin (HSA-NPS) revealed surprising differences in the number and distribution of naproxen binding sites. Bovine and leporine serum albumins possess three NPS binding sites, but ESA has only two. All three complexes of albumins studied here have two common naproxen locations, but BSA and LSA differ in the third NPS binding site. None of these binding sites coincides with the naproxen location in the HSA-NPS complex, which was obtained in the presence of other ligands besides naproxen. Even small differences in sequences of serum albumins from various species, especially in the area of the binding pockets, influence the affinity and the binding mode of naproxen to this transport protein.
© 2014 Wiley Periodicals, Inc.
Publication Date: 2014-04-29 PubMed ID: 24753230DOI: 10.1002/prot.24583Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The researchers analyzed the three-dimensional structure of complexes of serum albumins–proteins that carry substances in our blood–from cows, horses, and rabbits with the drug naproxen. They found that there are differences in the number and locations where naproxen attaches to these proteins between the different species and with humans.
Understanding Serum Albumin and Naproxen Complexes
- Serum albumin is a protein that is naturally abundant in our blood and helps transport a wide range of substances.
- Naproxen is a commonly used pain reliever that binds to serum albumin.
- The researchers present crystal structures of serum albumins from bovines (cows), equines (horses), and leporines (rabbits) in combination with naproxen.
Differences in Binding Sites
- The researchers found surprising differences in the number of binding sites where naproxen attaches to serum albumins from different species.
- Cow and rabbit serum albumins have three naproxen binding sites, but horse serum albumin only has two.
- All of the albumins studied have two common naproxen locations, but cow and rabbit albumins have a different location for the third binding site.
Comparison with Human Serum Albumin
- The researchers also compared the animal serum albumins with human serum albumin (HSA).
- Interestingly, none of the binding sites for naproxen on the animal albumins coincided with the binding site on HSA.
- This observation was made even when HSA was examined in the presence of other substances that also bind to it.
Significance of the Findings
- This study demonstrates that even small differences in the sequences of albumins between different species can impact how a drug like naproxen interacts with these proteins.
- Understanding these variations could be important in determining how the drug is transported in the body and contributes to its efficacy and potential side effects.
Cite This Article
APA
Bujacz A, Zielinski K, Sekula B.
(2014).
Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen.
Proteins, 82(9), 2199-2208.
https://doi.org/10.1002/prot.24583 Publication
Researcher Affiliations
- Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 4/10, 90-924, Lodz, Poland.
MeSH Terms
- Animals
- Anti-Inflammatory Agents, Non-Steroidal / chemistry
- Binding Sites
- Cattle
- Crystallography, X-Ray
- Horses
- Humans
- Models, Molecular
- Multiprotein Complexes / chemistry
- Multiprotein Complexes / ultrastructure
- Naproxen / chemistry
- Protein Binding
- Protein Conformation
- Rabbits
- Serum Albumin / chemistry
- Serum Albumin / ultrastructure
Citations
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