Journal of Developing Drugs
Open Access
ISSN: 2329-6631
+44 1478 350008
ISSN: 2329-6631
+44 1478 350008
Ouahab Ammar
Batna University, Algeria
Posters & Accepted Abstracts: J Develop Drugs
It is somehow easy to understand why it is still so controversial the mechanisms of cellular uptake of Cell-Penetrating Peptides (CPP). Although there is evidence that these peptides are capable of directly crossing the plasma membrane without any intermediate step, still several researchers claim that endocytosis is an intermediate step required for entry into the cells. It is well known that ionic interactions play a critical role for the binding to the plasma membrane and translocation of CPPs. A simulation of the interaction between Arginine-Glycine (RG)5 and Histidine-Glutamic Acid (HE)5, as well as with DOPC of the lipid bilayer was conducted in order to calculate the free binding energy. The results supported the data obtained in the in vitro release, cell uptake and cytotoxicity studies. The absolute value of binding energy of (RG)5 with (HE)5 was the highest, however a decrease in the pH was found to diminish this strong bond. Interestingly, the conjugation of (RG)5 to PEG-PLA copolymer increased the binding energy to DOPC. In summary, the peptides tend to interact with the cell membrane which facilitates the uptake in an energy and receptor independent manner as postulated by many researchers.
Email: ouahab.am@gmail.com