@ARTICLE{Golovina2013639,
author={Golovina, G.V. and Rychkov, G.N. and Ol'shevskaya, V.A. and Zaitsev, A.V. and Kalinin, V.N. and Kuzmin, V.A. and Shtil, A.A.},
title={Differential binding preference of methylpheophorbide a and its diboronated derivatives to albumin and low density lipoproteins},
journal={Anti-Cancer Agents in Medicinal Chemistry},
year={2013},
volume={13},
number={4},
pages={639-646},
doi={10.2174/1871520611313040012},
note={cited By 4},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84876711965&doi=10.2174%2f1871520611313040012&partnerID=40&md5=333724dbe983dd768e1fe5e937dedd6e},
affiliation={Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow 119334, Russian Federation; Petersburg Nuclear Physics Institute, National Research Center, The Kurchatov Institute Orlova Roscha, Gatchina 188300, Russian Federation; Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, 28 Vavilov Street, Moscow 119991, Russian Federation; Blokhin Cancer Center, Russian Academy of Medical Sciences, 24 Kashirskoye shosse, Moscow 115478, Russian Federation; St. Petersburg State Polytechnical University, 29 Polytechnicheskaya Street, St. Petersburg 195251, Russian Federation},
abstract={The tetrapyrrolic macrocycle and the functional groups at its periphery allow for a variety of modifications aimed at multifunctional therapeutic compounds. In particular, conjugation of boron polyhedra yields dual efficacy antitumor photo/radiosensitizers. Structural optimization of these agents presumes the identification of macromolecules that bind and transport boronated tetrapyrroles. Using spectroscopic methods we demonstrated that methylpheophorbide a forms complexes with serum albumin and low density lipoproteins (LDL) whereas two diboronated derivatives, 13(2),17(3)-[di(o-carboran-1-yl)methoxycarbonyl]pheophorbide a and 13(2),17(3)-[di(1-carba-closo-dodecaboran-1-yl)methoxycarbonyl]pheophorbide a, were capable of binding to LDL but not to albumin. Molecular modeling showed a mode of interaction of methylpheophorbide a with the amino acid residues in the albumin's hemin binding site. In contrast, for diboronated derivatives such interactions are sterically hindered by boron polyhedra, in line with experimentally determined lack of complex formation with albumin. These data strongly suggest that LDL might be the preferred carrier for polycarborane containing methylpheophorbide a derivatives. © 2013 Bentham Science Publishers.},
author_keywords={Albumin;  Carborane;  Low density lipoproteins;  Methylpheophorbide a;  Molecular modeling},
correspondence_address1={Golovina, G. V.; Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow 119334, Russian Federation; email: golovinagalina@yandex.ru},
issn={18715206},
pubmed_id={23343083},
language={English},
abbrev_source_title={Anti-Cancer Agents Med. Chem.},
document_type={Article},
source={Scopus},
}

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In particular, conjugation of boron polyhedra yields dual efficacy antitumor photo/radiosensitizers. Structural optimization of these agents presumes the identification of macromolecules that bind and transport boronated tetrapyrroles. Using spectroscopic methods we demonstrated that methylpheophorbide a forms complexes with serum albumin and low density lipoproteins (LDL) whereas two diboronated derivatives, 13(2),17(3)-[di(o-carboran-1-yl)methoxycarbonyl]pheophorbide a and 13(2),17(3)-[di(1-carba-closo-dodecaboran-1-yl)methoxycarbonyl]pheophorbide a, were capable of binding to LDL but not to albumin. Molecular modeling showed a mode of interaction of methylpheophorbide a with the amino acid residues in the albumin's hemin binding site. In contrast, for diboronated derivatives such interactions are sterically hindered by boron polyhedra, in line with experimentally determined lack of complex formation with albumin. These data strongly suggest that LDL might be the preferred carrier for polycarborane containing methylpheophorbide a derivatives. © 2013 Bentham Science Publishers.","author_keywords":"Albumin; Carborane; Low density lipoproteins; Methylpheophorbide a; Molecular modeling","correspondence_address1":"Golovina, G. V.; Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow 119334, Russian Federation; email: golovinagalina@yandex.ru","issn":"18715206","pubmed_id":"23343083","language":"English","abbrev_source_title":"Anti-Cancer Agents Med. Chem.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Golovina2013639,\r\nauthor={Golovina, G.V. and Rychkov, G.N. and Ol'shevskaya, V.A. and Zaitsev, A.V. and Kalinin, V.N. and Kuzmin, V.A. and Shtil, A.A.},\r\ntitle={Differential binding preference of methylpheophorbide a and its diboronated derivatives to albumin and low density lipoproteins},\r\njournal={Anti-Cancer Agents in Medicinal Chemistry},\r\nyear={2013},\r\nvolume={13},\r\nnumber={4},\r\npages={639-646},\r\ndoi={10.2174/1871520611313040012},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84876711965&doi=10.2174%2f1871520611313040012&partnerID=40&md5=333724dbe983dd768e1fe5e937dedd6e},\r\naffiliation={Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow 119334, Russian Federation; Petersburg Nuclear Physics Institute, National Research Center, The Kurchatov Institute Orlova Roscha, Gatchina 188300, Russian Federation; Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, 28 Vavilov Street, Moscow 119991, Russian Federation; Blokhin Cancer Center, Russian Academy of Medical Sciences, 24 Kashirskoye shosse, Moscow 115478, Russian Federation; St. Petersburg State Polytechnical University, 29 Polytechnicheskaya Street, St. Petersburg 195251, Russian Federation},\r\nabstract={The tetrapyrrolic macrocycle and the functional groups at its periphery allow for a variety of modifications aimed at multifunctional therapeutic compounds. In particular, conjugation of boron polyhedra yields dual efficacy antitumor photo/radiosensitizers. Structural optimization of these agents presumes the identification of macromolecules that bind and transport boronated tetrapyrroles. Using spectroscopic methods we demonstrated that methylpheophorbide a forms complexes with serum albumin and low density lipoproteins (LDL) whereas two diboronated derivatives, 13(2),17(3)-[di(o-carboran-1-yl)methoxycarbonyl]pheophorbide a and 13(2),17(3)-[di(1-carba-closo-dodecaboran-1-yl)methoxycarbonyl]pheophorbide a, were capable of binding to LDL but not to albumin. Molecular modeling showed a mode of interaction of methylpheophorbide a with the amino acid residues in the albumin's hemin binding site. In contrast, for diboronated derivatives such interactions are sterically hindered by boron polyhedra, in line with experimentally determined lack of complex formation with albumin. 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