OPTIMIZATION OF RECOMBINANT PROTEIN EXPRESSION FOR CELL-PENETRATING PEPTIDE FUSIONS TO PROTEIN CARGO

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dc.contributor.advisorKarlsson, Amy Jen_US
dc.contributor.authorAdhikari, Sayaneeen_US
dc.contributor.departmentChemical Engineeringen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.date.accessioned2017-09-14T05:48:17Z
dc.date.available2017-09-14T05:48:17Z
dc.date.issued2017en_US
dc.description.abstractRecombinant production of cell-penetrating peptides (CPPs) as fusions to protein “cargo” leads to low yields for some CPP-cargo fusions; thus, ways to enhance the recombinant expression of peptide-cargo fusions need to be identified. We optimized expression conditions for fusions of five CPPs (NPFSD, pVEC, SynB, histatin-5 and MPG) to the cargo proteins biotin carboxyl carrier protein (BCCP), maltose binding protein (MBP) and green fluorescent protein GFP. Glutathione-S-transferase was incorporated as a fusion partner to improve expression. In general, expression at 37 oC for 6 h and 10 h led 2 to the highest levels of expression for the different CPP-cargo constructs. The fusion of histatin-5 to GFP was purified, and its translocation into the fungal pathogen Candida albicans was studied. The purified protein translocated into the nearly 3% of C. albicans cells. These results provide the foundation for future studies to improve translocation of varied CPP-cargo fusions into C. albicans cells.en_US
dc.identifierhttps://doi.org/10.13016/M2J678X36
dc.identifier.urihttp://hdl.handle.net/1903/20020
dc.language.isoenen_US
dc.subject.pqcontrolledChemical engineeringen_US
dc.subject.pqcontrolledCellular biologyen_US
dc.subject.pqcontrolledBiologyen_US
dc.titleOPTIMIZATION OF RECOMBINANT PROTEIN EXPRESSION FOR CELL-PENETRATING PEPTIDE FUSIONS TO PROTEIN CARGOen_US
dc.typeThesisen_US

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