Quantification of the Binding of Insulin-like Growth Factor-I (IGF-I) and IGF Binding Protein-3 (IGFBP-3) Using Surface Plasmon Resonance

Simple item page
dc.contributor.authorCassino, Theresa Rachelen
dc.contributor.committeechairWilliams, Kimberly Forstenen
dc.contributor.committeememberVan Cott, Kevin E.en
dc.contributor.committeememberDessy, Raymond E.en
dc.contributor.departmentChemical Engineeringen
dc.date.accessioned2014-03-14T20:39:50Zen
dc.date.adate2002-06-20en
dc.date.available2014-03-14T20:39:50Zen
dc.date.issued2002-05-30en
dc.date.rdate2003-06-20en
dc.date.sdate2002-06-12en
dc.description.abstractInsulin-like growth factor-I is a small growth factor known to signal in a variety of mammalian cells through the IGF-I cell surface receptor (IGF-IR). A unique feature of the IGF-I system is the regulation of this binding by soluble IGF binding proteins. Recent studies from our laboratory show that there is a pH dependence in the association of IGF-I with the cell surface in the presence of IGFBP-3 which suggested increased association of IGF-I with IGFBP-3 at low pH. We studied cell free interaction of IGF-I and IGFBP-3 as a function of pH using surface plasmon resonance (SPR) in order to understand the mechanism that causes the increased association. In our studies three different SPR instruments with different surfaces for immobilization of one of the binding partners were used: a Leica Bio-SPR 9000 with a low molecular weight carboxymethylated dextran (CMD) surface, a BIAcore 2000 with a high molecular weight CMD surface and a Leica SPR 2001 Alpha with a planar mixed self-assembled monolayer (mSAM) surface. Since the experimental system we used was transport sensitive, only the mSAM surface, under optimized conditions, produced results that fit to a single site model. Results suggest that use of CMD layers for immobilization of one partner of a high-affinity binding complex can result in transport limited binding for which simple analysis is inappropriate. Future studies are planned to expand the work with the mSAM surface to elucidate whether a significant difference between the binding parameters as a function of pH exists.en
dc.description.degreeMaster of Scienceen
dc.identifier.otheretd-06122002-115345en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-06122002-115345/en
dc.identifier.urihttp://hdl.handle.net/10919/33531en
dc.publisherVirginia Techen
dc.relation.haspartTRCassinoThesis.pdfen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectBiosensoren
dc.subjectInsulin-like Growth Factor Binding Protein-3 (IGFen
dc.subjectSurface Plasmon Resonanceen
dc.subjectInsulin-like Growth Factor-I (IGF-I)en
dc.subjectBinding Affinityen
dc.subjectGrowth Factoren
dc.titleQuantification of the Binding of Insulin-like Growth Factor-I (IGF-I) and IGF Binding Protein-3 (IGFBP-3) Using Surface Plasmon Resonanceen
dc.typeThesisen
thesis.degree.disciplineChemical Engineeringen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.levelmastersen
thesis.degree.nameMaster of Scienceen

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
TRCassinoThesis.pdf
Size:
2.26 MB
Format:
Adobe Portable Document Format
Download

Collections

Masters Theses