Binding Affinity of Synthetic Cannabinoids to Human Serum Albumin: Site Characterization and Interaction Insights Article Swipe
Rita M. G. Santos
,
Rita Lima
,
Sara Cravo
,
Pedro Alexandrino Fernandes
,
Fernando Remião
,
Carla Fernandes
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.3390/ph18040581
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.3390/ph18040581
Background/Objectives: High-performance affinity chromatography (HPAC) was used to investigate the binding affinity of a series of synthetic cannabinoids, a widely abused class of new psychoactive substances, to human serum albumin (HSA) and obtain insights into the binding sites. To better understand the recognition mechanisms, molecular docking studies were conducted. Methods: Binding affinity was assessed through zonal elution approach Additionally, displacement chromatography with site-specific probes provided insights into the HSA binding sites of five synthetic cannabinoids. Results: That these drugs exhibit extensive binding to HSA, with values ranging from 98.7% to 99.9%. Competition for site I was observed between warfarin and four synthetic cannabinoids (5F-AMB, AB-PINACA, AMB-FUBINACA, and AB-CHMINACA). Furthermore, AB-CHMINACA also competed with L-tryptophan for site II. The binding affinity of all synthetic cannabinoids increased in the presence of (S)-ibuprofen. Molecular docking studies supported the experimental findings, reinforcing the insights gained. Conclusions: The key novelty of this study lies in analyzing, for the first time, the binding affinity of synthetic cannabinoids to HSA through HPAC and molecular docking. These results may improve our understanding of their toxicokinetic behavior and help in predicting possible competitive interactions that could influence HSA binding and, consequently, their activity and toxicity. This study is the first to describe the binding affinity of synthetic cannabinoids to HSA, elucidate their recognition mechanisms, identify binding sites, and characterize their interactions with the protein.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.3390/ph18040581
- https://www.mdpi.com/1424-8247/18/4/581/pdf?version=1744799604
- OA Status
- gold
- Cited By
- 1
- References
- 63
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4409505729
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4409505729Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.3390/ph18040581Digital Object Identifier
- Title
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Binding Affinity of Synthetic Cannabinoids to Human Serum Albumin: Site Characterization and Interaction InsightsWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-04-16Full publication date if available
- Authors
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Rita M. G. Santos, Rita Lima, Sara Cravo, Pedro Alexandrino Fernandes, Fernando Remião, Carla FernandesList of authors in order
- Landing page
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https://doi.org/10.3390/ph18040581Publisher landing page
- PDF URL
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https://www.mdpi.com/1424-8247/18/4/581/pdf?version=1744799604Direct link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://www.mdpi.com/1424-8247/18/4/581/pdf?version=1744799604Direct OA link when available
- Concepts
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Human serum albumin, Synthetic cannabinoids, Binding site, Chemistry, Docking (animal), Cannabinoid, Plasma protein binding, Affinity chromatography, Computational biology, Biochemistry, Biology, Receptor, Medicine, Nursing, EnzymeTop concepts (fields/topics) attached by OpenAlex
- Cited by
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1Total citation count in OpenAlex
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2025: 1Per-year citation counts (last 5 years)
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63Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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