Cited by 376Protein Interaction Studies and Fluorescence AnalysisComputational Drug Discovery MethodsDrug Transport and Resistance Mechanisms

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Interactive Association of Drugs Binding to Human Serum Albumin

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Yang, Feng, Zhang, Yao, Liang, Hong·2014·International Journal of Molecular Sciences

DOI 10.3390/ijms15033580PMC PMC3975355

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Abstract

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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BindingDB Entry 50009676: Discovery and Optimization of Salicylic Acid-Derived Sulfonamide Inhibitors of the WD Repeat-Containing Protein 5-MYC Protein-Protein Interaction.
BindingDB (2021) · UC San Diego · doi:10.7270/q2b85cm0
Molecular Interactions between Styrene Oligomers and Human Serum Albumin: A Multiscale Computational Study of a Plastic-Derived Environmental Contaminant
Gonçalves, V. A., Amaral, J. L., França, V. L. B., Carvalho, H. F., Brunaldi, K., Caetano, E. W. S., & Freire, V. N. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.6c04082

Authors: Yang, F., Zhang, Y., & Liang, H.
Affiliations: Guangxi Normal University (CN)
Corresponding author: Yang, Feng
Liang, Hong
ORCID: Yang, Feng
Zhang, Yao
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)
DOI: 10.3390/ijms15033580
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: cc-by
creativecommons.org/licenses/by/3.0/ (vor)
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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Interactive Association of Drugs Binding to Human Serum Albumin

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