ERRATUM TO: Methods to Study the Role of the Glycocalyx in the Uptake of Cell-Penetrating Peptides

2015 ◽  
pp. E1-E1
Author(s):  
Samuel Schmidt ◽  
Rike Wallbrecher ◽  
Toin H. van Kuppevelt ◽  
Roland Brock
Keyword(s):  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals Role of charge and hydrophobicity in translocation of cell‐penetrating peptides into Candida albicans cells

AIChE Journal ◽  
2019 ◽  
Vol 65 (12) ◽  
Author(s):  
Zifan Gong ◽  
Mary T. Doolin ◽  
Sayanee Adhikari ◽  
Kimberly M. Stroka ◽  
Amy J. Karlsson
Keyword(s):  
Candida Albicans ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals The role of endocytosis on the uptake kinetics of luciferin-conjugated cell-penetrating peptides

2012 ◽  
Vol 1818 (3) ◽  
pp. 502-511 ◽  
Author(s):  
Imre Mäger ◽  
Kent Langel ◽  
Taavi Lehto ◽  
Emelía Eiríksdóttir ◽  
Ülo Langel
Keyword(s):  
Cell Penetrating Peptides ◽  
Uptake Kinetics ◽  
Cell Penetrating ◽  
Kinetics Of

scholarly journals Role of Cell-Penetrating Peptides in Intracellular Delivery of Peptide Nucleic Acids Targeting Hepadnaviral Replication

2017 ◽  
Vol 9 ◽  
pp. 162-169 ◽  
Author(s):  
Bénédicte Ndeboko ◽  
Narayan Ramamurthy ◽  
Guy Joseph Lemamy ◽  
Catherine Jamard ◽  
Peter E. Nielsen ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Peptide Nucleic Acids ◽  
Intracellular Delivery ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals The role of tryptophans on the cellular uptake and membrane interaction of arginine-rich cell penetrating peptides

2015 ◽  
Vol 1848 (2) ◽  
pp. 593-602 ◽  
Author(s):  
Marie-Lise Jobin ◽  
Marine Blanchet ◽  
Sarah Henry ◽  
Stéphane Chaignepain ◽  
Claude Manigand ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Cell Penetrating Peptides ◽  
Membrane Interaction ◽  
Cell Penetrating

Role of cell-surface carbohydrates and plasma membrane components in the internalization of cell-penetrating peptides

2010 ◽  
Vol 15 (23-24) ◽  
pp. 1101-1101
Author(s):  
Chérine Bechara ◽  
Chen-Yu Jiao ◽  
Fabienne Burlina ◽  
Isabel D. Alves ◽  
Gérard Chassaing ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating ◽  
Membrane Components ◽  
Surface Carbohydrates

scholarly journals Ionpair-π interactions favor cell penetration of arginine/tryptophan-rich cell-penetrating peptides

2019 ◽  
Author(s):  
Astrid Walrant ◽  
Antonio Bauzá ◽  
Claudia Girardet ◽  
Isabel D. Alves ◽  
Sophie Lecomte ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Density Functional ◽  
Molecular Mechanisms ◽  
Cell Penetrating Peptides ◽  
Membrane Phospholipids ◽  
Active Peptides ◽  
Π Interactions ◽  
Cell Penetrating ◽  
Membrane Active Peptides

AbstractCell-penetrating peptides (CPPs) internalization can occur both by endocytosis and direct translocation through the cell membrane. These different entry routes suggest that molecular partners at the plasma membrane, phospholipids or glycosaminoglycans (GAGs), bind CPPs with different affinity or selectivity. The analysis of sequence-dependent interactions of CPPs with lipids and GAGs should lead to a better understanding of the molecular mechanisms underlying their internalization. CPPs are short sequences generally containing a high number of basic arginines and lysines and sometimes aromatic residues, in particular tryptophans. Tryptophans are crucial residues in membrane-active peptides, because they are important for membrane interaction. Membrane-active peptides often present facial amphiphilicity, which also promote the interaction with lipid bilayers. To study the role of Trp and facial amphiphilicity in cell interaction and penetration of CPPs, a nonapeptide series containing only Arg, Trp or D-Trp residues at different positions was designed. Our quantitative study indicates that to maintain/increase the uptake efficiency, Arg can be advantageously replaced by Trp in the nonapeptides. The presence of Trp in oligoarginines increases the uptake in cells expressing GAGs at their surface, when it only compensates for the loss of Arg and maintains similar peptide uptake in GAG-deficient cells. In addition, we show that facial amphiphilicity is not required for efficient uptake of these nonapeptides. Thermodynamic analyses point towards a key role of Trp that highly contributes to the binding enthalpy of complexes formation. Density functional theory (DFT) analysis highlights that salt bridge-π interactions play a crucial role for the GAG-dependent entry mechanisms.

scholarly journals Region-Dependent Role of Cell-Penetrating Peptides in Insulin Absorption Across the Rat Small Intestinal Membrane

2015 ◽  
Vol 17 (6) ◽  
pp. 1427-1437 ◽  
Author(s):  
El-Sayed Khafagy ◽  
Ruisha Iwamae ◽  
Noriyasu Kamei ◽  
Mariko Takeda-Morishita
Keyword(s):  
Cell Penetrating Peptides ◽  
Insulin Absorption ◽  
Intestinal Membrane ◽  
Cell Penetrating ◽  
Small Intestinal
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