Dissertation/Thesis Abstract

Temperature controlled cellular internalization of hybrid peptides
by Oh, Myungeun, M.S., California State University, Long Beach, 2016, 86; 10144830
Abstract (Summary)

This study examined various hybrid peptides that possess both collagen [(POG)n] and cell penetrating peptides (CPP) [(RRG)n or Rn] sequences. The hybrid peptides were able to fold into triple helical conformation when the surrounding temperature was lower than their transition temperature (Tm) which resulted in cellular internalization. The peptide that lacked collagen [(POG)n] domain failed to penetrate the cell. The hybrid peptide under study, FL7V1, was shown to have the ideal Tm (17.3°C) for the potential purpose as a drug carrier. In vitro 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). In vivo study of FL7V1 with P. leidyi corresponded with the results of in vitro study at constant and gradient temperature.

Indexing (document details)
Advisor: Slowinska, Katarzyna
Commitee: McAbee, Douglas, Slowinska, Katarzyna, Weers, Paul M. M.
School: California State University, Long Beach
Department: Chemistry and Biochemistry
School Location: United States -- California
Source: MAI 56/01M(E), Masters Abstracts International
Subjects: Cellular biology, Biochemistry
Keywords: Cell penetrating peptides, Cellular internalization, Collagen mimetic peptides, Drug delivery, Hybrid peptides, Temperature controlled targeting
Publication Number: 10144830
ISBN: 978-1-369-00410-6
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