Cited by 66Protein Interaction Studies and Fluorescence AnalysisNanoparticle-Based Drug DeliveryAdvanced Drug Delivery Systems

Cationic charge‐dependent hepatic delivery of amidated serum albumin

Ma, Shen-Feng, Nishikawa, Makiya, Katsumi, Hidemasa, Yamashita, Fumiyoshi, Hashida, Mitsuru·2005·Journal of Controlled Release

Abstract

To obtain a quantitative correlation between the physicochemical properties of amidated bovine serum albumin (BSA) and their tissue distribution characteristics for the development of targeted delivery of proteins, BSA was amidated with hexamethylenediamine (HMD) or ethylenediamine (ED) to obtain cationized BSAs. Their structural changes were examined by spectroscopic and electrophoretic techniques then their tissue distribution was studied in mice. Circular dichroism (CD) and fluorescence measurements showed that spectroscopic changes occurred as the number of free NH2 groups increased. Capillary electrophoresis revealed a linear relationship between the mobility and the increased number of free NH2 groups. 111In-cationized BSAs were rapidly taken up by liver, but HMD-BSA showed a faster uptake than ED-BSA with a similar number of free NH2 groups, suggesting that the diamine reagent with a longer carboxyl side chain results in more efficient hepatic targeting. The hepatic uptake clearance (CL(liver)) of both derivatives increased significantly with a decrease in electrophoretic mobility (mu(ep)) towards the anode and reached a plateau at low electrophoretic mobility. The electrophoretic mobility is an appropriate indicator of the degree of amidation, which was closely correlated with the hepatic uptake clearance. The correlation between the mobility and the clearance shows that a low degree of amidation is sufficient for efficient hepatic targeting of proteins.

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Crossref · 10.1016/j.jconrel.2004.11.006

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  • The breakdown of serum albumin is complicated by the fact that after oxidation, glycation, or binding of pro-oxidative substances, serum albumin loses its antioxidant capacity and is more rapidly degraded than reduced unbound serum albumin.

    “The breakdown of serum albumin is complicated by the fact that after oxidation, glycation, or binding of pro‐oxidative substances, serum albumin loses its antioxidant capacity and is more rapidly degraded than reduced unbound serum albumin.79, 80, 81, 82, 83”

    From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [80]

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Authors
Ma, S.-F., Nishikawa, M., Katsumi, H., Yamashita, F., & Hashida, M.
Affiliations
Kyoto University (JP)
Corresponding author
Hashida, Mitsuru
Venue
Journal of Controlled Release
Publisher
Elsevier BV
Published
2005-02
Volume
102
Issue
3
Pages
583-594
ISSN
0168-3659 (ISSN-L)
OpenAlex
W2036485362
Cited by
66
References
33
Citations by year
2026: 1 · 2025: 1 · 2022: 4 · 2021: 1 · 2020: 5 · 2019: 6 · 2018: 7 · 2017: 7 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 2 · 2012: 3
FWCI
1.31
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Controlled Release (publishedVersion)
  • PubMed (publishedVersion)
Funders
Ministry of Education, Culture, Sports, Science and Technology
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Physical Sciences › Materials Science › Biomaterials › Nanoparticle-Based Drug Delivery
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmaceutical Science › Advanced Drug Delivery Systems
Keywords
hepatic targeting, protein delivery, hexamethylenediamine, ethylenediamine, electrophoretic mobility, tissue distribution
MeSH terms
Amides, Animals, Cations, Electrophoresis, Liver, Male, Serum Albumin, Drug Delivery Systems, Mice

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