Show simple item record Crider, SE Holbrook, RJ Franz, KJ
dc.coverage.spatial England 2011-06-21T17:27:13Z 2010-01
dc.identifier.citation Metallomics, 2010, 2 (1), pp. 74 - 83
dc.description.abstract Platinum therapeutic agents are widely used in the treatment of several forms of cancer. Various mechanisms for the transport of the drugs have been proposed including passive diffusion across the cellular membrane and active transport via proteins. The copper transport protein Ctr1 is responsible for high affinity copper uptake but has also been implicated in the transport of cisplatin into cells. Human hCtr1 contains two methionine-rich Mets motifs on its extracellular N-terminus that are potential platinum-binding sites: the first one encompasses residues 7-14 with amino acid sequence Met-Gly-Met-Ser-Tyr-Met-Asp-Ser and the second one spans residues 39-46 with sequence Met-Met-Met-Met-Pro-Met-Thr-Phe. In these studies, we use liquid chromatography and mass spectrometry to compare the binding interactions between cisplatin, carboplatin and oxaliplatin with synthetic peptides corresponding to hCtr1 Mets motifs. The interactions of cisplatin and carboplatin with Met-rich motifs that contain three or more methionines result in removal of the carrier ligands of both platinum complexes. In contrast, oxaliplatin retains its cyclohexyldiamine ligand upon platinum coordination to the peptide.
dc.format.extent 74 - 83
dc.language eng
dc.language.iso en_US en_US
dc.relation.ispartof Metallomics
dc.relation.isversionof 10.1039/b916899k
dc.subject Amino Acid Motifs
dc.subject Amino Acid Sequence
dc.subject Amino Acid Substitution
dc.subject Antineoplastic Agents
dc.subject Cation Transport Proteins
dc.subject Chromatography, Liquid
dc.subject Humans
dc.subject Mass Spectrometry
dc.subject Methionine
dc.subject Molecular Sequence Annotation
dc.subject Molecular Sequence Data
dc.subject Norleucine
dc.subject Organoplatinum Compounds
dc.subject Peptides
dc.title Coordination of platinum therapeutic agents to met-rich motifs of human copper transport protein1.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US 2010-00-00 en_US
duke.description.endpage 83 en_US
duke.description.issue 1 en_US
duke.description.startpage 74 en_US
duke.description.volume 2 en_US
dc.relation.journal Metallomics en_US
pubs.issue 1
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Chemistry
pubs.publication-status Published
pubs.volume 2
dc.identifier.eissn 1756-591X

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