| dc.identifier.uri | http://hdl.handle.net/11401/77118 | |
| dc.description.sponsorship | This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree. | en_US |
| dc.format | Monograph | |
| dc.format.medium | Electronic Resource | en_US |
| dc.language.iso | en_US | |
| dc.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
| dc.type | Dissertation | |
| dcterms.abstract | Chapter 1 Receptors on cell membrane surfaces play critical roles for the cell to communicate with the outside environment by forming protein complexes. Therefore, identifying protein partners in the complex is of major importance. We are developed ROMP (ring opening metasthesis polymerization) polymers as tools for identifying the partners. The polymers bear several functional groups such as ligands for binding to a known receptor, benzophenone group to covalently connect the partner proteins to the polymer, and alkyne for click reaction to attach biotins. With this functionalized polymer, possible protein partners can be purified and analyzed by peptide mass finger printing. To optimize the function of this polymer and the experimental procedure, the α vβ 3-MMP2, was used as a model system. Chapter 4 A new prodrug for selective cancer therapy that uses the increased activities of histone deacetylase (HDAC) and protease cathepsin L (CTSL) in cancer cells was synthesized. Puromycine coupled with acetylated lysine group is not cytotoxic because the free amine is masked. We optimized the synthesis and the purification of puromycine coupled with acetylated lysine group to obtain highly pure (<95 %) product for testing in vivo. Chapter 5 Early diagnosis of metastasis and prevention of metastasis is a major obstacle in cancer treatment due to the lack of imaging probes specific to early stage cancer. MT1-MMP, a membrane anchored matrix metalloproteinase, is upregulated in invasive human breast cancers even in early stages. The PEX domain of MT1-MMP is required for migration of aggressive cancer cells.Peptides mimicking 8 amino acids of the outermost β -strand of the blades from the PEX domain of MT1-MMP successfully inhibited the migration of aggressive cancer cells. This peptide was coupled to 18F-FDG for PET imaging and testing of the conjugate in vitro and in vivo. | |
| dcterms.available | 2017-09-20T16:52:00Z | |
| dcterms.contributor | Laughlin, Scott | en_US |
| dcterms.contributor | Sampson, Nicole S. | en_US |
| dcterms.contributor | Ojima, Iwao | en_US |
| dcterms.contributor | Hayman, Michael. | en_US |
| dcterms.creator | Lee, Siyeon | |
| dcterms.dateAccepted | 2017-09-20T16:52:00Z | |
| dcterms.dateSubmitted | 2017-09-20T16:52:00Z | |
| dcterms.description | Department of Chemistry. | en_US |
| dcterms.extent | 216 pg. | en_US |
| dcterms.format | Application/PDF | en_US |
| dcterms.format | Monograph | |
| dcterms.identifier | http://hdl.handle.net/11401/77118 | |
| dcterms.issued | 2015-08-01 | |
| dcterms.language | en_US | |
| dcterms.provenance | Made available in DSpace on 2017-09-20T16:52:00Z (GMT). No. of bitstreams: 1
Lee_grad.sunysb_0771E_11835.pdf: 21659757 bytes, checksum: a999d92cc69bf21cda642318dea6c660 (MD5)
Previous issue date: 2014 | en |
| dcterms.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
| dcterms.subject | Chemistry | |
| dcterms.title | Development of Photo-Affinity based ROMP Polymers for Identifying Receptors on Cell Surface | |
| dcterms.type | Dissertation | |
