New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs
A new chimeric gene ApE1 encoding the receptor-binding domain of the human alpha-fetoprotein fused to a sequence of 22 glutamic acid residues was constructed. A new bacterial producer strain E. coli SHExT7 ApE1 was selected for ApE1 production in a soluble state. A simplified method was developed to...
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2012-01-01
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Series: | Journal of Biomedicine and Biotechnology |
Online Access: | http://dx.doi.org/10.1155/2012/469756 |
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doaj-4046576a88fe4911bd8454faeb56a38c2020-11-25T02:19:30ZengHindawi LimitedJournal of Biomedicine and Biotechnology1110-72431110-72512012-01-01201210.1155/2012/469756469756New Protein Vector ApE1 for Targeted Delivery of Anticancer DrugsN. V. Pozdniakova0N. V. Gorokhovets1N. V. Gukasova2A. V. Bereznikova3E. S. Severin4Centre for Convergence of Nano-, Bio-, Information and Cognitive Sciences and Technologies (Kurchatov NBIC Centre), National Research Centre “Kurchatov Institute”, Academician Kurchatov Square, 1, Building 348, Moscow 123182, RussiaCentre for Convergence of Nano-, Bio-, Information and Cognitive Sciences and Technologies (Kurchatov NBIC Centre), National Research Centre “Kurchatov Institute”, Academician Kurchatov Square, 1, Building 348, Moscow 123182, RussiaCentre for Convergence of Nano-, Bio-, Information and Cognitive Sciences and Technologies (Kurchatov NBIC Centre), National Research Centre “Kurchatov Institute”, Academician Kurchatov Square, 1, Building 348, Moscow 123182, RussiaBiological Faculty, Lomonosov Moscow State University, Vorobyovy Gory, 1, Building 12, Moscow 119234, RussiaBiological Faculty, Lomonosov Moscow State University, Vorobyovy Gory, 1, Building 12, Moscow 119234, RussiaA new chimeric gene ApE1 encoding the receptor-binding domain of the human alpha-fetoprotein fused to a sequence of 22 glutamic acid residues was constructed. A new bacterial producer strain E. coli SHExT7 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.http://dx.doi.org/10.1155/2012/469756 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
N. V. Pozdniakova N. V. Gorokhovets N. V. Gukasova A. V. Bereznikova E. S. Severin |
spellingShingle |
N. V. Pozdniakova N. V. Gorokhovets N. V. Gukasova A. V. Bereznikova E. S. Severin New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs Journal of Biomedicine and Biotechnology |
author_facet |
N. V. Pozdniakova N. V. Gorokhovets N. V. Gukasova A. V. Bereznikova E. S. Severin |
author_sort |
N. V. Pozdniakova |
title |
New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs |
title_short |
New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs |
title_full |
New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs |
title_fullStr |
New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs |
title_full_unstemmed |
New Protein Vector ApE1 for Targeted Delivery of Anticancer Drugs |
title_sort |
new protein vector ape1 for targeted delivery of anticancer drugs |
publisher |
Hindawi Limited |
series |
Journal of Biomedicine and Biotechnology |
issn |
1110-7243 1110-7251 |
publishDate |
2012-01-01 |
description |
A new chimeric gene ApE1 encoding the receptor-binding domain of the human alpha-fetoprotein fused to a sequence of 22 glutamic acid residues was constructed. A new bacterial producer strain E. coli SHExT7 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. |
url |
http://dx.doi.org/10.1155/2012/469756 |
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