Author

Author Type

Graduate Student

Date of Award

2011

Document Type

Thesis

Publication Status

Version of Record

Submission Date

October 2026

Abstract

Cell penetrating peptides (CPPs) have drawn the attention of researchers due to their ability to internalize large cargos into cells including cancer cells. The mechanism(s) with which the peptides enter the cell, however, is/are not clear and full of controversy. The peptide conformations and their microenvironment in live cells had been unknown until the development of a technique developed in our lab. As a first demonstration of principle, penetratin, a 16-residue CPP derived from the Antennapedia homeodomain protein of Drosophila, was measured in single, living melanoma cells. Carbon-13 labeling of the Phe residue of penetratin was used to shift the intense aromatic ring-breathing vibrational mode from 1003 to 967 cm-1, thereby enabling the peptide to be traced in cells. Difference spectroscopy and principal components analysis (PCA) were used independently to resolve the Raman spectrum of the peptide from the background cellular Raman signals.

Extent

xvii, 191 p. : ill. (some col.)

Comments

by Jing Ye.|Thesis (Ph.D.)--Florida Atlantic University, 2011.|Includes bibliography.|Electronic reproduction. Boca Raton, Fla., 2011. Mode of access: World Wide Web.|by Jing Ye.

Identifier

FADT3342344

Format

pdf

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