Page 1 |
Save page Remove page | Previous | 1 of 55 | Next |
|
small (250x250 max)
medium (500x500 max)
large ( > 500x500)
Full Resolution
All (PDF)
|
This page
All
Subset |
i
COMPARISON OF CELLULAR UPTAKE OF
ARGININE-RICH CELL-PENETRATING PEPTIDES
by
Ling Ren
_______________________
A Thesis Presented to the
FACULTY OF THE GRADUATE SCHOOL
UNIVERSITY OF SOUTHERN CALIFORNIA
In Partial Fulfillment of the
Requirements for the Degree
MASTER OF SCIENCE
(PHARMACEUTICAL SCIENCES)
May 2009
Copyright 2009 Ling Ren
Object Description
| Title | Comparison of cellular uptake of arginine-rich cell-penetrating peptides |
| Author | Ren, Ling |
| Author email | lren@usc.edu; lingren1776@gmail.com |
| Degree | Master of Science |
| Document type | Thesis |
| Degree program | Pharmaceutical Sciences |
| School | School of Pharmacy |
| Date defended/completed | 2009-04-14 |
| Date submitted | 2009 |
| Restricted until | Unrestricted |
| Date published | 2009-05-04 |
| Advisor (committee chair) | Shen, Wei-Chiang |
| Advisor (committee member) |
Wang, Clay Okamoto, Curtis |
| Abstract | In this study, five arginine-rich peptides YGR6, YGR6E6, YG(RE)6, YGR6G6 and YG(RG)6 were engineered for investigating the roles of positive charges and sequence of cationic amino acid residues in their membrane transduction activity. The results demonstrated that the positive charges are crucial factors to achieve high level of cellular uptake. YGR6E6, YG(RE)6, YGR6G6 and YG(RG)6 showed less cellular uptake compared with YGR6. Especially, in the neutralized form, the surface-binding and internalization of YGR6E6 and YG(RE)6 dramatically decreased. However, YGR6G6 and YG(RG)6 still showed comparable uptake profile in CHO cells as compared to YGR6. A comparison between YGR6E6 and YG(RE)6 or YGR6G6 and YG(RG)6 indicated that the clustering of positive charges was important for initiating the membrane transduction activity of arginine-containing peptides. Cellular uptake assay was also conducted to investigate the ratio of endocytosis versus membrane transduction. Results from this study indicated that all these peptides were mainly internalized by membrane transduction rather than endocytosis. |
| Keyword | cell-penetrating peptide; arginine rich; transduction; endocytosis; drug delivery |
| Language | English |
| Part of collection | University of Southern California dissertations and theses |
| Publisher (of the original version) | University of Southern California |
| Place of publication (of the original version) | Los Angeles, California |
| Publisher (of the digital version) | University of Southern California. Libraries |
| Provenance | Electronically uploaded by the author |
| Type | texts |
| Legacy record ID | usctheses-m2175 |
| Rights | Ren, Ling |
| Repository name | Libraries, University of Southern California |
| Repository address | Los Angeles, California |
| Repository email | http://www.usc.edu/isd/libraries/services/ask_a_librarian/email/ |
| Filename | etd-ren-2695 |
| Archival file | uscthesesreloadpub_Volume23/etd-ren-2695-0.pdf |
Description
| Title | Page 1 |
| Full text | i COMPARISON OF CELLULAR UPTAKE OF ARGININE-RICH CELL-PENETRATING PEPTIDES by Ling Ren _______________________ A Thesis Presented to the FACULTY OF THE GRADUATE SCHOOL UNIVERSITY OF SOUTHERN CALIFORNIA In Partial Fulfillment of the Requirements for the Degree MASTER OF SCIENCE (PHARMACEUTICAL SCIENCES) May 2009 Copyright 2009 Ling Ren |
Comments
Post a Comment for Page 1

