<p> This study examined various hybrid peptides that possess both collagen [(POG)<sub>n</sub>] and cell penetrating peptides (CPP) [(RRG)<sub>n</sub> or R<sub>n</sub>] sequences. The hybrid peptides were able to fold into triple helical conformation when the surrounding temperature was lower than their transition temperature (T<sub>m</sub>) which resulted in cellular internalization. The peptide that lacked collagen [(POG)<sub>n</sub>] domain failed to penetrate the cell. The hybrid peptide under study, FL7V1, was shown to have the ideal T<sub>m</sub> (17.3°C) for the potential purpose as a drug carrier. <i>In vitro</i> study of FL6V1 with temperature gradient showed cellular internalization at low temperatures (10°C-20°C) while no uptake was achieved at high temperatures (24°C-32°C). <i> In vivo</i> study of FL7V1 with <i>P. leidyi</i> corresponded with the results of <i>in vitro</i> study at constant and gradient temperature.</p>
| Identifer | oai:union.ndltd.org:PROQUEST/oai:pqdtoai.proquest.com:10144830 |
| Date | 11 October 2016 |
| Creators | Oh, Myungeun |
| Publisher | California State University, Long Beach |
| Source Sets | ProQuest.com |
| Language | English |
| Detected Language | English |
| Type | thesis |
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