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The Photolytic Activity of Poly‐Arginine Cell Penetrating Peptides Conjugated to Carboxy‐tetramethylrhodamine is Modulated by Arginine Residue Content and Fluorophore Conjugation Site
Author(s) -
Muthukrishnan Nandhini,
Donovan Stephen,
Pellois JeanPhilippe
Publication year - 2014
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/php.12288
Subject(s) - fluorophore , chemistry , biophysics , peptide , arginine , cell penetrating peptide , biochemistry , endocytic cycle , conjugate , membrane , fluorescence , cell , biology , amino acid , endocytosis , mathematical analysis , physics , mathematics , quantum mechanics
Abstract Upon light irradiation, Fluorophore–cell‐penetrating peptide (Fl‐ CPP ) conjugates can disrupt the integrity of biological membranes. This activity can in turn be used to photoinduce the disruption of endocytic organelles and promote the delivery of entrapped macromolecules such as proteins or RNA s into live cells. Recent mechanistic studies have shown that ROS production by the fluorophore and a latent lytic ability of CPP s act in synergy to elicit photolysis. However, how the structure of fluorophore‐ CPP conjugates impacts this synergistic activity remains unclear. Herein, using red blood cells ( RBC s) as a model of biological membranes, we show that the number of arginine residues in a CPP as well as the position of fluorophore with respect to the CPP dramatically affect the photolytic activity of a fluorophore‐ CPP conjugate. These factors should therefore be considered for the development of effective photoinducible delivery agents.