The DOI matches its Crossref record; 119 of the 121 references it cites were found in a registry or an index.
Interactive Association of Drugs Binding to Human Serum Albumin
Open accessAbstract
Human serum albumin (HSA) is an abundant plasma protein, which attracts great interest in the pharmaceutical industry since it can bind a remarkable variety of drugs impacting their delivery and efficacy and ultimately altering the drug's pharmacokinetic and pharmacodynamic properties. Additionally, HSA is widely used in clinical settings as a drug delivery system due to its potential for improving targeting while decreasing the side effects of drugs. It is thus of great importance from the viewpoint of pharmaceutical sciences to clarify the structure, function, and properties of HSA-drug complexes. This review will succinctly outline the properties of binding site of drugs in IIA subdomain within the structure of HSA. We will also give an overview on the binding characterization of interactive association of drugs to human serum albumin that may potentially lead to significant clinical applications.
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“In conjunction with an exterior aqueous environment, large proteins like HSA that have multiple hydrophobic binding sites can provide an amphiphilic environment in which different protein residues interact with the polar headgroups and hydrophobic perfluorotails of PFAS simultaneously [57].”
From In-Vitro and In-Silico Assessment of Per- and Polyfluoroalkyl Substances (PFAS) in Aqueous Film-Forming Foam (AFFF) Binding to Human Serum Albumin (2021) · cites this paper as [57]
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Cites
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Flagged first, then by citations
2 of the 121 references couldn’t be matched to a known paper.
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- Tillement, 2006, Drug binding to blood proteins: Characteristics roles and pathophysiological changes, Bull. Acad. Natl. Med., 190, 935
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Lomis, N., Westfall, S., Farahdel, L., Malhotra, M., Shum‐Tim, D., & Prakash, S. (2016) · Nanomaterials · doi:10.3390/nano6060116 · Cited by 188
Targeted Delivery Methods for Anticancer Drugs
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Siddiqui, S., Ameen, F., Rehman, S. U., Sarwar, T., & Tabish, M. (2021) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2021.116200 · Cited by 173
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Metadata
- Authors
- Yang, F., Zhang, Y., & Liang, H.
- Affiliations
- Guangxi Normal University (CN)
- Corresponding author
- Yang, Feng
- Liang, Hong
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2014-02-27
- Volume
- 15
- Issue
- 3
- Pages
- 3580-3595
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC3975355
- OpenAlex
- W1973788406
- Cited by
- 376
- References
- 121
- Citations by year
- 2026: 26 · 2025: 40 · 2024: 38 · 2023: 33 · 2022: 48 · 2021: 26 · 2020: 35 · 2019: 38 · 2018: 24 · 2017: 25 · 2016: 29 · 2015: 14
- FWCI
- 2.14
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (31060121, 20130403-1, 21171043, 2013GXNSFGA019010)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- human serum albumin, drug binding, binding sites, drug delivery systems, pharmacokinetics, pharmacodynamics
- MeSH terms
- Binding Sites, Pharmaceutical Preparations, Humans, Kinetics, Models, Molecular, Protein Binding, Serum Albumin, Molecular Structure, Protein Structure, Secondary, Protein Structure, Tertiary
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