The photolytic activity of poly-arginine cell penetrating peptides conjugated to carboxy-tetramethylrhodamine is modulated by arginine residue content and fluorophore conjugation site. Academic Article uri icon

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 RNAs into live cells. Recent mechanistic studies have shown that ROS production by the fluorophore and a latent lytic ability of CPPs 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 (RBCs) 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.

published proceedings

  • Photochem Photobiol

author list (cited authors)

  • Muthukrishnan, N., Donovan, S., & Pellois, J.

citation count

  • 11

complete list of authors

  • Muthukrishnan, Nandhini||Donovan, Stephen||Pellois, Jean-Philippe

publication date

  • September 2014

publisher