New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs
| Autor: | Anastasia V. Bereznikova, N. V. Gorokhovets, N. V. Pozdniakova, N. V. Gukasova, Severin Es |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Article Subject
Receptors Peptide Recombinant Fusion Proteins Health Toxicology and Mutagenesis lcsh:Biotechnology Molecular Sequence Data lcsh:Medicine Antineoplastic Agents Plasma protein binding Chimeric gene Biology medicine.disease_cause chemistry.chemical_compound Cell Line Tumor lcsh:TP248.13-248.65 Escherichia coli Genetics medicine Humans Amino Acid Sequence Cloning Molecular Binding site Receptor Molecular Biology Peptide sequence Drug Carriers Binding Sites Polyglutamic acid lcsh:R General Medicine Glutamic acid Polyglutamic Acid chemistry Biochemistry Molecular Medicine alpha-Fetoproteins Fluorescein-5-isothiocyanate Protein Binding Research Article Biotechnology |
| Zdroj: | Journal of Biomedicine and Biotechnology, Vol 2012 (2012) Journal of Biomedicine and Biotechnology |
| ISSN: | 1110-7251 1110-7243 |
| Popis: | A new chimeric geneApE1encoding the receptor-binding domain of the humanalpha-fetoprotein fused to a sequence of 22 glutamic acid residues was constructed. A new bacterial producer strainE. coliSHExT7 ApE1 was selected for ApE1 production in a soluble state. A simplified method was developed to purify ApE1 from bacterial biomass. It was shown that the new vector protein selectively interacts with AFP receptors on the tumor cell surface and can be efficiently accumulated in tumor cells. In addition, ApE1 was shown to be stable in storage and during its chemical modification. An increased number of carboxyl groups in the molecule allows the production of cytotoxic compound conjugates with higher drug-loading capacity and enhanced tumor targeting potential. |
| Databáze: | OpenAIRE |
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