Targeted delivery via avidin fusion protein: Intracellular fate of biotinylated doxorubicin derivative and cellular uptake kinetics and biodistribution of biotinylated liposomes

Soininen, Suvi K.; Lehtolainen-Dalkilic, Pauliina; Karppinen, Tanja; Puustinen, Tiina; Dragneva, Galina; Kaikkonen, Minna U.; Jauhiainen, Marjo; Allart, Brigitte; Selwood, David L.; Wirth, Thomas; Lesch, Hanna P.; Määttä, Ann-Marie; Mönkkönen, Jukka; Ylä‐Herttuala, Seppo; Ruponen, Marika

doi:10.1016/j.ejps.2012.09.001

Cited by 21 publications

(37 citation statements)

References 47 publications

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“…By utilizing the strong affinity of SAV to biotin, biotin derivatives, such as biotinylated antibodies or biotinylated doxorubicin, have been developed . Therefore, our results suggest that SAV‐LA can be used to modify the surface of exosomes with functional molecules, such as the biotin derivatives described above.…”

Section: Discussionmentioning

confidence: 89%

Quantitative Analysis of Tissue Distribution of the B16BL6-Derived Exosomes Using a Streptavidin-Lactadherin Fusion Protein and Iodine-125-Labeled Biotin Derivative After Intravenous Injection in Mice

Morishita

Takahashi

Nishikawa

et al. 2015

Journal of Pharmaceutical Sciences

243

179

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Section: Discussionmentioning

confidence: 89%

Quantitative Analysis of Tissue Distribution of the B16BL6-Derived Exosomes Using a Streptavidin-Lactadherin Fusion Protein and Iodine-125-Labeled Biotin Derivative After Intravenous Injection in Mice

Morishita

Takahashi

Nishikawa

et al. 2015

Journal of Pharmaceutical Sciences

243

179

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“…However, cancer cells display an array of common traits to allow their permanent growth and spreading, such as angiogenesis promotion, release of matrix-degrading enzymes, and high expression of receptors and carriers for nutrients [8]. Namely, biotin receptors have been found to be highly active and overexpressed in cancer cells [9,10]. Moreover, emerging evidence points to the participation of biotin in cell signaling, gene expression, and chromatin structure in cell proliferation [11].…”

Section: Introductionmentioning

confidence: 99%

Biotinylated polyurethane-urea nanoparticles for targeted theranostics in human hepatocellular carcinoma

et al. 2015

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Over the past years, significant efforts have been devoted to explore novel drug delivery and detection strategies for simultaneous therapy and diagnostics. The development of biotinylated polyurethane-urea nanoparticles as theranostic nanocarriers for targeted drug and plasmid delivery, for fluorescence detection of human hepatocellular carcinoma cells, is described herein. These targeted nanoparticles are specifically designed to incorporate biotin into the polymeric matrix, since many tumor types overexpress receptors for biotin as a mechanism to boost uncontrolled cell growth. The obtained nanoparticles were spherical, exhibited an average diameter ranging 110-145 nm, and showed no cytotoxicity in healthy endothelial cells. Biotinylated nanoparticles are selectively incorporated into the perinuclear and nuclear area of the human hepatocellular carcinoma cell line, HepG2, in division, but not into growing, healthy, human endothelial cells. Indeed, the simultaneous incorporation of the anticancer drugs, phenoxodiol or sunitinib, together with plasmid DNA encoding green fluorescent protein, into these nanoparticles allows a targeted pharmacological antitumor effect and furthermore, selective transfection of a reporter gene, to detect these cancer cells. The combined targeted therapy and detection strategy described here could be exploited for liver cancer therapy and diagnostics, with a moderate safety profile, and may also be a potential tool for other types of cancer.

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“…The cells of mammals such as human, mouse, rat, and Chinese hamster serve as hosts for the expression of fusion proteins of biotin-binding proteins and antibodies or other pharmaceutical proteins. [11][12][13][14][15][16][17][18] Given that the codon preferences among these mammals are similar, there is a good chance that mam-tam2A and mam-tam2B would also be highly expressed in the cells of these other mammals. One or two amino acids of mam-tam2A and mam-tam2B could be changed to create derivatives with a lower isoelectric point, 7) reversible biotin-binding capability, 8) or extremely high thermal stability.…”

Section: Discussionmentioning

confidence: 99%

“…In many cases, the fusion proteins were expressed in mammalian cells so that the characteristics of the fusion partners, which are quite often mammalian proteins, would be fully retained. [11][12][13][14][15][16][17][18] Monoclonal antibodies against targets such as receptors and surface proteins of cancer cells are popular fusion partners, because these fusion proteins can attach to the cancer cells to deliver the biotinylated therapeutics.…”

mentioning

confidence: 99%

High-level expression of tamavidin 2 in human cells by codon-usage optimization

Takakura

Katayama

Nagata

2015

Bioscience, Biotechnology, and Biochemistry

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Tamavidin 2 is a fungal protein that binds to biotin with an extremely high affinity. Tamavidin 2 is superior to avidin or streptavidin in terms of its low-level non-specific binding and high-level thermal stability. However, the gene for tamavidin 2 is highly expressed in Escherichia coli but not in mammalian cells, restricting its application as an affinity tag in mammalian cells. Here, we optimized the codon usage of tamavidin 2 for human cells and found that the resultant mutant expressed tamavidin 2 at approximately 30-fold higher level compared with the native gene. The protein thus produced in human cells could be purified by iminobiotin affinity chromatography, bound tightly to biotin, and was stable at high temperature (82 °C). This powerful technology for high-level expression of tamavidin 2 in mammalian cells will be of value in evaluating various fusion proteins produced in mammalian cells for numerous applications.

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Targeted delivery via avidin fusion protein: Intracellular fate of biotinylated doxorubicin derivative and cellular uptake kinetics and biodistribution of biotinylated liposomes

Cited by 21 publications

References 47 publications

Quantitative Analysis of Tissue Distribution of the B16BL6-Derived Exosomes Using a Streptavidin-Lactadherin Fusion Protein and Iodine-125-Labeled Biotin Derivative After Intravenous Injection in Mice

Quantitative Analysis of Tissue Distribution of the B16BL6-Derived Exosomes Using a Streptavidin-Lactadherin Fusion Protein and Iodine-125-Labeled Biotin Derivative After Intravenous Injection in Mice

Biotinylated polyurethane-urea nanoparticles for targeted theranostics in human hepatocellular carcinoma

High-level expression of tamavidin 2 in human cells by codon-usage optimization

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