Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin
Studies on the interactions between metallodrugs and human serum albumin (HSA), as carrier for drugs and biological molecules, are extremely important to design and discover new drugs. The interaction of three novel synthesized complexes of [Pd(phen)(R-gly)]NO 3 , where R-gly is methyl-, propyl-, an...
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| Veröffentlicht in: | Combinatorial chemistry & high throughput screening 2014-01, Vol.17 (9), p.781-789 |
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| creator | Moghadam, Mahboube Eslami Saidifar, Maryam Rostami-Charati, Faramarz Ajloo, Davoud Ghadamgahi, Maryam |
| description | Studies on the interactions between metallodrugs and human serum albumin (HSA), as carrier for drugs and
biological molecules, are extremely important to design and discover new drugs. The interaction of three novel
synthesized complexes of [Pd(phen)(R-gly)]NO 3 , where R-gly is methyl-, propyl-, and amyl-glycine and phen is 1,10-
phenanthroline, with HSA were investigated using spectroscopic studies in combination with a molecular dynamic
simulation. These water soluble complexes can denature HSA at ~50 µM. According to the results obtained for the
isothermal titration at 27 and 37°C, it was found that there are 10, 8, and 6 binding sites (g) for methyl-, propyl-, and
amyl-glycine complexes on the HSA with positive cooperativity in binding, respectively. Also, the binding and
thermodynamic parameters were analyzed. We found a good consistency between secondary structure and simulation data
with spectroscopic studies, and the experimental data are confirmed by molecular simulation results. In addition, the
results related to helix, beta sheets, and coil percentages revealed that all complexes decrease the helix structure and
increase the beta structure; and that the amyl derivative is more effective in denaturing the HSA structure. |
| doi_str_mv | 10.2174/1386207317666140926124647 |
| format | Article |
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biological molecules, are extremely important to design and discover new drugs. The interaction of three novel
synthesized complexes of [Pd(phen)(R-gly)]NO 3 , where R-gly is methyl-, propyl-, and amyl-glycine and phen is 1,10-
phenanthroline, with HSA were investigated using spectroscopic studies in combination with a molecular dynamic
simulation. These water soluble complexes can denature HSA at ~50 µM. According to the results obtained for the
isothermal titration at 27 and 37°C, it was found that there are 10, 8, and 6 binding sites (g) for methyl-, propyl-, and
amyl-glycine complexes on the HSA with positive cooperativity in binding, respectively. Also, the binding and
thermodynamic parameters were analyzed. We found a good consistency between secondary structure and simulation data
with spectroscopic studies, and the experimental data are confirmed by molecular simulation results. In addition, the
results related to helix, beta sheets, and coil percentages revealed that all complexes decrease the helix structure and
increase the beta structure; and that the amyl derivative is more effective in denaturing the HSA structure.</description><identifier>ISSN: 1386-2073</identifier><identifier>EISSN: 1875-5402</identifier><identifier>DOI: 10.2174/1386207317666140926124647</identifier><identifier>PMID: 25262751</identifier><language>eng</language><publisher>United Arab Emirates: Bentham Science Publishers Ltd</publisher><subject>Humans ; Molecular Dynamics Simulation ; Molecular Structure ; Organometallic Compounds - chemical synthesis ; Organometallic Compounds - chemistry ; Palladium - chemistry ; Serum Albumin - chemistry ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Thermodynamics</subject><ispartof>Combinatorial chemistry & high throughput screening, 2014-01, Vol.17 (9), p.781-789</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b442t-97e27f704c651434ba4fc0e4296be02e51ecfc2d014f4ffc46135a3893d7c8913</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25262751$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moghadam, Mahboube Eslami</creatorcontrib><creatorcontrib>Saidifar, Maryam</creatorcontrib><creatorcontrib>Rostami-Charati, Faramarz</creatorcontrib><creatorcontrib>Ajloo, Davoud</creatorcontrib><creatorcontrib>Ghadamgahi, Maryam</creatorcontrib><title>Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin</title><title>Combinatorial chemistry & high throughput screening</title><addtitle>CCHTS</addtitle><description>Studies on the interactions between metallodrugs and human serum albumin (HSA), as carrier for drugs and
biological molecules, are extremely important to design and discover new drugs. The interaction of three novel
synthesized complexes of [Pd(phen)(R-gly)]NO 3 , where R-gly is methyl-, propyl-, and amyl-glycine and phen is 1,10-
phenanthroline, with HSA were investigated using spectroscopic studies in combination with a molecular dynamic
simulation. These water soluble complexes can denature HSA at ~50 µM. According to the results obtained for the
isothermal titration at 27 and 37°C, it was found that there are 10, 8, and 6 binding sites (g) for methyl-, propyl-, and
amyl-glycine complexes on the HSA with positive cooperativity in binding, respectively. Also, the binding and
thermodynamic parameters were analyzed. We found a good consistency between secondary structure and simulation data
with spectroscopic studies, and the experimental data are confirmed by molecular simulation results. In addition, the
results related to helix, beta sheets, and coil percentages revealed that all complexes decrease the helix structure and
increase the beta structure; and that the amyl derivative is more effective in denaturing the HSA structure.</description><subject>Humans</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular Structure</subject><subject>Organometallic Compounds - chemical synthesis</subject><subject>Organometallic Compounds - chemistry</subject><subject>Palladium - chemistry</subject><subject>Serum Albumin - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Thermodynamics</subject><issn>1386-2073</issn><issn>1875-5402</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUtv1DAUhSMEog_4CyjsymLAdhw7WVZTaEcqAmlgbTnOzYzBj-BHp7Nnx5_G0yndsfK1znfse8-tqrcYvSeY0w-46RhBvMGcMYYp6gnDhDLKn1WnuOPtoqWIPC914RYH8KQ6i_EHQojhhr6sTkhLGOEtPq3-fPYGVDYy1Fd7J61W9Vrbck_au1q6sV7PoFLwUfm5iCt3BzHpzVH3U732FurlPvnk74v-VRojR53txWr1rl56Oxu4h1h8CYJUD66dTtv6Jlvp6jWEbOtLM2Sr3avqxSRNhNeP53n1_dPHb8ubxe2X69Xy8nYxUErSoudA-MQRVazFtKGDpJNCQEnPBkAEWgxqUmREmE50mhQtQ7ey6fpm5KrrcXNeXRzfnYP_lcs4wuqooDTuwOcoMCt5MsY5L2h_RFVJIAaYxBy0lWEvMBKHXYj_7qJ43zx-kwcL45PzX_gF-H0EBnBpK21UGpyCJ3Cb0ix2u52AHOCnjFA2lYTyVvgZXA6m1CVWl8S8ncUGXAAhQ9LKgNAxuofexKE5cedNtiAwPwgZRC_iLDcgeIebv05Rubk</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Moghadam, Mahboube Eslami</creator><creator>Saidifar, Maryam</creator><creator>Rostami-Charati, Faramarz</creator><creator>Ajloo, Davoud</creator><creator>Ghadamgahi, Maryam</creator><general>Bentham Science Publishers Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20140101</creationdate><title>Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin</title><author>Moghadam, Mahboube Eslami ; Saidifar, Maryam ; Rostami-Charati, Faramarz ; Ajloo, Davoud ; Ghadamgahi, Maryam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b442t-97e27f704c651434ba4fc0e4296be02e51ecfc2d014f4ffc46135a3893d7c8913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Humans</topic><topic>Molecular Dynamics Simulation</topic><topic>Molecular Structure</topic><topic>Organometallic Compounds - chemical synthesis</topic><topic>Organometallic Compounds - chemistry</topic><topic>Palladium - chemistry</topic><topic>Serum Albumin - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moghadam, Mahboube Eslami</creatorcontrib><creatorcontrib>Saidifar, Maryam</creatorcontrib><creatorcontrib>Rostami-Charati, Faramarz</creatorcontrib><creatorcontrib>Ajloo, Davoud</creatorcontrib><creatorcontrib>Ghadamgahi, Maryam</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Combinatorial chemistry & high throughput screening</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moghadam, Mahboube Eslami</au><au>Saidifar, Maryam</au><au>Rostami-Charati, Faramarz</au><au>Ajloo, Davoud</au><au>Ghadamgahi, Maryam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin</atitle><jtitle>Combinatorial chemistry & high throughput screening</jtitle><addtitle>CCHTS</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>17</volume><issue>9</issue><spage>781</spage><epage>789</epage><pages>781-789</pages><issn>1386-2073</issn><eissn>1875-5402</eissn><abstract>Studies on the interactions between metallodrugs and human serum albumin (HSA), as carrier for drugs and
biological molecules, are extremely important to design and discover new drugs. The interaction of three novel
synthesized complexes of [Pd(phen)(R-gly)]NO 3 , where R-gly is methyl-, propyl-, and amyl-glycine and phen is 1,10-
phenanthroline, with HSA were investigated using spectroscopic studies in combination with a molecular dynamic
simulation. These water soluble complexes can denature HSA at ~50 µM. According to the results obtained for the
isothermal titration at 27 and 37°C, it was found that there are 10, 8, and 6 binding sites (g) for methyl-, propyl-, and
amyl-glycine complexes on the HSA with positive cooperativity in binding, respectively. Also, the binding and
thermodynamic parameters were analyzed. We found a good consistency between secondary structure and simulation data
with spectroscopic studies, and the experimental data are confirmed by molecular simulation results. In addition, the
results related to helix, beta sheets, and coil percentages revealed that all complexes decrease the helix structure and
increase the beta structure; and that the amyl derivative is more effective in denaturing the HSA structure.</abstract><cop>United Arab Emirates</cop><pub>Bentham Science Publishers Ltd</pub><pmid>25262751</pmid><doi>10.2174/1386207317666140926124647</doi><tpages>9</tpages></addata></record> |
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| source | MEDLINE; IngentaConnect Free/Open Access Journals |
| subjects | Humans Molecular Dynamics Simulation Molecular Structure Organometallic Compounds - chemical synthesis Organometallic Compounds - chemistry Palladium - chemistry Serum Albumin - chemistry Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Thermodynamics |
| title | Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin |
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