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

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

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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Crossref · 10.3390/ijms15033580

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  • 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.

    “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]

    The section “Binding Site of Drugs in IIA Subdomain of HSA” (page unavailable) describes a hydrophobic pocket containing polar residues and a residue interacting with a fatty acid’s carboxylate group. This supports the proposed mixed-polarity environment, but the paper does not describe residues simultaneously interacting with PFAS headgroups and perfluorotails. Its reference to a PFOS transport study does not establish that specific mechanism. (LLM, conf=0.86)

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2 of the 121 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

  1. [21]Tillement J.P. Duché J.C. Barré J. Drug binding to blood proteins: Characteristics roles and pathophysiological changes Bull. Acad. Natl. Med. 2006 190 935 946 17195618
  2. [49]Bhattacharya A.A. Grüne T. Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin J. Mol. Biol. 2000 303 721 732 11061971

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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)
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
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
  • Physical Sciences › Computer Science › Computational Theory and Mathematics › 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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