Re-evaluating the role of strongly charged sequences in amphipathic cell-penetrating peptides: A fluorescence study using Pep-1

摘要: Cell-penetrating peptides (CPPs) are able to translocate across biological membranes and deliver bioactive proteins. Cellular uptake intracellular distribution of CPPs is commonly evaluated with fluorescent labels, which can alter peptide properties. The effect carboxyfluorescein label in the Lys-rich domain amphipathic CPP pep-1, was compared non-labelled pep-1 vitro vivo. A reduced membrane affinity an endosomal-dependent translocation mechanism, at variance were detected. Therefore, charged not a mere enabler adsorption but has crucial role pathway pep-1.