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dc.identifier.urihttp://hdl.handle.net/1951/59759
dc.identifier.urihttp://hdl.handle.net/11401/71320
dc.description.sponsorshipThis work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.en_US
dc.formatMonograph
dc.format.mediumElectronic Resourceen_US
dc.language.isoen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dc.typeThesis
dcterms.abstractMatrix metalloproteinases (MMPs) play an important role in cancer progression by degrading extracellular matrix components, promoting tumor cell migration, and thus enhancing tumor metastasis. Several generations of anticancer drug were designed to inhibit the proteolytic functions of MMPs, but these drugs failed in clinic trails due to lack of selectivity. This study focused on the hemopexin domain of MMP-9, a nonproteolytic domain, which is essential for MMP-9 regulated tumor cell migration. Compared with the catalytic domain of MMPs, fewer amino acids are conserved between the hemopexin domains of MMP family members. This difference provides the principle basis for identification of inhibitors targeting the hemopexin domain with high selectivity and specificity. An in silico docking approach was employed to screen for novel small-molecule compound that bind to the hemopexin domain of MMP-9. Seven computational hits were evaluated in biochemical binding assays. Of these, 4 compounds were identified that have micromolar affinities for the hemopexin domain of MMP-9
dcterms.available2013-05-22T17:35:06Z
dcterms.available2015-04-24T14:47:02Z
dcterms.contributorSampson, Nicole Sen_US
dcterms.contributorRizzo, Robert Cen_US
dcterms.contributorBoon, Elizabeth.en_US
dcterms.creatorLi, Zhu
dcterms.dateAccepted2013-05-22T17:35:06Z
dcterms.dateAccepted2015-04-24T14:47:02Z
dcterms.dateSubmitted2013-05-22T17:35:06Z
dcterms.dateSubmitted2015-04-24T14:47:02Z
dcterms.descriptionDepartment of Chemistryen_US
dcterms.extent74 pg.en_US
dcterms.formatMonograph
dcterms.formatApplication/PDFen_US
dcterms.identifierLi_grad.sunysb_0771M_11040en_US
dcterms.identifierhttp://hdl.handle.net/1951/59759
dcterms.identifierhttp://hdl.handle.net/11401/71320
dcterms.issued2012-08-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2013-05-22T17:35:06Z (GMT). No. of bitstreams: 1 Li_grad.sunysb_0771M_11040.pdf: 3398598 bytes, checksum: 4f03e9d2d4e0fe2f400560e5c0ce62d7 (MD5) Previous issue date: 1en
dcterms.provenanceMade available in DSpace on 2015-04-24T14:47:02Z (GMT). No. of bitstreams: 3 Li_grad.sunysb_0771M_11040.pdf.jpg: 1894 bytes, checksum: a6009c46e6ec8251b348085684cba80d (MD5) Li_grad.sunysb_0771M_11040.pdf.txt: 89368 bytes, checksum: 44d92ff3a5adeb3c3ac66b5b516214dd (MD5) Li_grad.sunysb_0771M_11040.pdf: 3398598 bytes, checksum: 4f03e9d2d4e0fe2f400560e5c0ce62d7 (MD5) Previous issue date: 1en
dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectChemistry--Biochemistry
dcterms.subjectanticancer drug, docking, MMP-9
dcterms.titleIdentification of small molecules that bind to the hemopexin domain of matrix metalloproteinase-9
dcterms.typeThesis


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