Intrinsically Cell-Permeable Miniature Proteins Based on a Minimal Cationic PPII Motif

Author(s)

Alanna S. Schepartz, Yale University
Douglas S. Daniels, University of DaytonFollow

Document Type

Article

Publication Date

11-6-2007

Publication Source

Journal of the American Chemical Society

Abstract

Cell-penetrating peptides (CPPs) provide promising tools for the cellular delivery of molecular cargos ranging in size from small molecules and peptides to proteins and quantum dots. CPPs are typically cationic and/or amphipathic sequences that are unstructured or α-helical. We expand the repertoire of cell-penetrating motifs by designing encodable CPPs possessing type-II polyproline (PPII) helical structure. These motifs surpass the uptake efficiency of existing CPPs and are not cytotoxic at concentrations 100 times greater than that necessary for delivery. By replacing the PPII helix of a miniature protein, the motif can endow intrinsic cell permeability without increasing molecular size.

Inclusive pages

14578-14579

ISBN/ISSN

0002-7863

Comments

Featured in "Revamped Molecular Transporters Shine," Chemical & Engineering News, Vol. 85, No. 43 (2007).

Copyright

Copyright © 2007, American Chemical Society

Publisher

American Chemical Society

Volume

129

Peer Reviewed

yes

Issue

47

Keywords

Flow cytometry, Peptides and proteins, Fluorescence, Protein structure, Toxicity

eCommons Citation

Schepartz, Alanna S. and Daniels, Douglas S., "Intrinsically Cell-Permeable Miniature Proteins Based on a Minimal Cationic PPII Motif" (2007). Chemistry Faculty Publications. 92.
https://ecommons.udayton.edu/chm_fac_pub/92