Source:http://linkedlifedata.com/resource/pubmed/id/21113330
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-12-7
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pubmed:abstractText |
The interactions of ?-arene-Ru(II)-chloroquine complexes with human serum albumin (HSA), apotransferrin and holotransferrin have been studied by circular dichroism (CD) and UV-Visible spectroscopies, together with isothermal titration calorimetry (ITC). The data for [Ru(?(6)-p-cymene)(CQ)(H(2)O)Cl]PF(6) (1), [Ru(?(6)-benzene)(CQ)(H(2)O)Cl]PF(6) (2), [Ru(?(6)-p-cymene)(CQ)(H(2)O)(2)][PF(6)](2) (3), [Ru(?(6)-p-cymene)(CQ)(en)][PF(6)](2) (4), [Ru(?(6)-p-cymene)(?(6)-CQDP)][BF(4)](2) (5) (CQ: chloroquine; DP: diphosphate; en: ethylenediamine), in comparison with CQDP and [Ru(?(6)-p-cymene)(en)Cl][PF(6)] (6) as controls demonstrate that 1, 2, 3, and 5, which contain exchangeable ligands, bind to HSA and to apotransferrin in a covalent manner. The interaction did not affect the ?-helical content in apotransferrin but resulted in a loss of this type of structure in HSA. The binding was reversed in both cases by a decrease in pH and in the case of the Ru-HSA adducts, also by addition of chelating agents. A weaker interaction between complexes 4 and 6 and HSA was measured by ITC but was not detectable spectroscopically. No interactions were observed for complexes 4 and 6 with apotransferrin or for CQDP with either protein. The combined results suggest that the arene-Ru(II)-chloroquine complexes, known to be active against resistant malaria and several lines of cancer cells, also display a good transport behavior that makes them good candidates for drug development.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/1S06GM 076168-04,
http://linkedlifedata.com/resource/pubmed/grant/GM 008078,
http://linkedlifedata.com/resource/pubmed/grant/GM 06298,
http://linkedlifedata.com/resource/pubmed/grant/R01-AI060014,
http://linkedlifedata.com/resource/pubmed/grant/S06 GM076168-040004,
http://linkedlifedata.com/resource/pubmed/grant/SC1 GM089558-02
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antimalarials,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Organometallic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Ruthenium,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/apotransferrin,
http://linkedlifedata.com/resource/pubmed/chemical/holotransferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1873-3344
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-45
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21113330-Antimalarials,
pubmed-meshheading:21113330-Antineoplastic Agents,
pubmed-meshheading:21113330-Apoproteins,
pubmed-meshheading:21113330-Calorimetry,
pubmed-meshheading:21113330-Chloroquine,
pubmed-meshheading:21113330-Circular Dichroism,
pubmed-meshheading:21113330-Drug Interactions,
pubmed-meshheading:21113330-Humans,
pubmed-meshheading:21113330-Molecular Structure,
pubmed-meshheading:21113330-Organometallic Compounds,
pubmed-meshheading:21113330-Ruthenium,
pubmed-meshheading:21113330-Serum Albumin,
pubmed-meshheading:21113330-Transferrin
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pubmed:year |
2011
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pubmed:articleTitle |
Interactions of arene-Ru(II)-chloroquine complexes of known antimalarial and antitumor activity with human serum albumin (HSA) and transferrin.
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pubmed:affiliation |
Chemistry Department, Brooklyn College and The Graduate Center, The City University of New York, 2900 Bedford Avenue, Brooklyn, NY 11210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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