Author/Authors :
Shirani، Ali نويسنده Faculty of Advanced Medical Sciences, Department of Medical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran. , , Shahbazi Mojarrad، Javid نويسنده Biotechnology Research Center and Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran. , , Mussa Farkhani، Samad نويسنده Research Center for Pharmaceutical Nanotechnology and Department of Medical Nanotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran. , , Yari Khosroshahi، Ahmad نويسنده Biotechnology Research Center and Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran. , , Zakeri-Milani، Parvin نويسنده Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran. , , Samadi، Naser نويسنده , , Sharifi، Simin نويسنده Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran. , , mohammadi، samaneh نويسنده , , Valizadeh، Hadi نويسنده Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran. ,
Abstract :
Purpose: Cell-penetrating peptides (CPPs) are used for delivering drugs and other
macromolecular cargo into living cells. In this paper, we investigated the relationship
between the structural/physicochemical properties of four new synthetic peptides containing
arginine-tryptophan in terms of their cell membrane penetration efficiency.
Methods: The peptides were prepared using solid phase synthesis procedure using FMOC
protected amino acids. Fluorescence-activated cell sorting and fluorescence imaging were used
to evaluate uptake efficiency. Prediction of the peptide secondary structure and estimation of
physicochemical properties was performed using the GOR V method and MPEx 3.2 software
(Wimley-White scale, helical wheel projection and total hydrophobic moment).
Results: Our data showed that the uptake efficiency of peptides with two tryptophans at the Cand
N-terminus were significantly higher (about 4-fold) than that of peptides containing three
tryptophans at both ends. The distribution of arginine at both ends also increased the uptake
efficiency 2.52- and 7.18-fold, compared with arginine distribution at the middle of peptides.
Conclusion: According to the obtained results the value of transfer free energies of peptides
from the aqueous phase to membrane bilayer could be a good predictor for the cellular
uptake efficiency of CPPs.
