scholarly journals Cargo self-assembly rescues affinity of cell-penetrating peptides to lipid membranes

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Andreas Weinberger ◽  
Vivien Walter ◽  
Sarah R. MacEwan ◽  
Tatiana Schmatko ◽  
Pierre Muller ◽  
...  
Keyword(s):  
Self Assembly ◽  
Lipid Membranes ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals Magnetic Nanoparticle Assisted Self-assembly of Cell Penetrating Peptides-Oligonucleotides Complexes for Gene Delivery

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Moataz Dowaidar ◽  
Hani Nasser Abdelhamid ◽  
Mattias Hällbrink ◽  
Krista Freimann ◽  
Kaido Kurrikoff ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Self Assembly ◽  
Magnetic Nanoparticle ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals Self-assembly of mitochondria-specific peptide amphiphiles amplifying lung cancer cell death through targeting the VDAC1–hexokinase-II complex

2019 ◽  
Vol 7 (30) ◽  
pp. 4706-4716 ◽  
Author(s):  
Dan Liu ◽  
Angelina Angelova ◽  
Jianwen Liu ◽  
Vasil M. Garamus ◽  
Borislav Angelov ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cell Death ◽  
Cancer Cell ◽  
Self Assembly ◽  
Cell Penetrating Peptides ◽  
Lung Cancer Cell ◽  
Hexokinase Ii ◽  
Cancer Cell Death ◽  
Cell Penetrating ◽  
Specific Peptide

Novel cell-penetrating peptides self-assemble into ellipsoid-shape nanostructures which amplified the apoptotic stimuli by weakening the VDAC1–HK-II interaction.

scholarly journals The single GUV method for revealing the functions of antimicrobial, pore-forming toxin, and cell-penetrating peptides or proteins

2014 ◽  
Vol 16 (30) ◽  
pp. 15752-15767 ◽  
Author(s):  
Md. Zahidul Islam ◽  
Jahangir Md. Alam ◽  
Yukihiro Tamba ◽  
Mohammad Abu Sayem Karal ◽  
Masahito Yamazaki
Keyword(s):  
Rate Constants ◽  
Lipid Membranes ◽  
Pore Formation ◽  
Cell Penetrating Peptides ◽  
Elementary Processes ◽  
Cell Penetrating

The single GUV method provides detailed information on the elementary processes of peptide/protein-induced pore formation in lipid membranes and the entry of peptides into a GUV; specifically, the GUV method provides the rate constants of these processes.

all-D proline-rich cell-penetrating peptides: a preliminary in vivo internalization study

2007 ◽  
Vol 35 (4) ◽  
pp. 794-796 ◽  
Author(s):  
S. Pujals ◽  
E. Sabidó ◽  
T. Tarragó ◽  
E. Giralt
Keyword(s):  
Self Assembly ◽  
Laser Scanning ◽  
White Blood Cells ◽  
Cell Penetrating Peptides ◽  
Laser Scanning Microscopy ◽  
Confocal Laser ◽  
Cell Penetrating ◽  
Peptide Derivatives ◽  
Degradation Problem

Proline-rich cell-penetrating peptides, particularly the SAP (sweet arrow peptide), (VRLPPP)3, have been proposed to be useful intracellular delivery vectors, as a result of their lack of cytotoxicity combined with their capacity to be internalized by cells. A common limitation of the therapeutic use of peptides is metabolic instability. In general, peptides are quickly degraded by proteases upon entry into the bloodstream. The use of all-D-peptide derivatives is emerging as a fruitful strategy to circumvent this degradation problem. In this context, we report on the internalization behaviour, protease-resistance enhancement and self-assembly properties of an all-D version of SAP [(vrlppp)3]. The cellular uptake of (vrlppp)3 was evaluated in an in vivo assay in mice. Both flow cytometry and confocal laser-scanning microscopy experiments showed that a carboxyfluoresceinated version of the molecule, carboxyfluorescein–(vrlppp)3, is internalized rapidly in white blood cells and kidney cells. Significant fluorescence was also detected in other organs such as the spleen and the liver. Finally, the toxicity of (vrlppp)3 was examined, and no significant differences in the main biochemical parameters nor in weight were detected compared with controls.

Label-free quantification of cell-penetrating peptide translocation into liposomes

2016 ◽  
Vol 8 (23) ◽  
pp. 4608-4616 ◽  
Author(s):  
Marie-Lise Jobin ◽  
Isabel D. Alves
Keyword(s):  
Small Molecules ◽  
Lipid Membranes ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating Peptide ◽  
Label Free ◽  
Label Free Quantification ◽  
Cell Penetrating ◽  
Free Quantification ◽  
Peptide Translocation

Cell penetrating peptides (CPPs) are small molecules capable of crossing lipid membranes and transporting cargos of varied sizes and nature inside cells.

Thermodynamics of cell penetrating peptides on lipid membranes: sequence and membrane acidity regulate surface binding

2020 ◽  
Vol 22 (40) ◽  
pp. 23399-23410
Author(s):  
Pedro G. Ramírez ◽  
Mario G. Del Pópolo ◽  
Jorge A. Vila ◽  
Gabriel S. Longo
Keyword(s):  
Lipid Membranes ◽  
Cell Penetrating Peptides ◽  
Surface Binding ◽  
Cell Penetrating ◽  
Acidic Lipids

Acidic lipids respond to pH in ways that fully promote or deplete the surface accumulation of cell penetrating peptides.

scholarly journals Cell Penetrating Peptide-Based Self-Assembly for PD-L1 Targeted Tumor Regression

2021 ◽  
Vol 22 (24) ◽  
pp. 13314
Author(s):  
Feng Guo ◽  
Junfeng Ke ◽  
Zhengdong Fu ◽  
Wenzhao Han ◽  
Liping Wang
Keyword(s):  
Self Assembly ◽  
Tumor Regression ◽  
Cell Penetrating Peptides ◽  
Electronic Interactions ◽  
Continuous Sequence ◽  
Cell Penetrating ◽  
Good Biocompatibility ◽  
Covalently Linked

Cell penetrating peptides (CPPs) are peptides that can directly adapt to cell membranes and then permeate into cells. CPPs are usually covalently linked to the surface of nanocarriers to endow their permeability to the whole system. However, hybrids with lipids or polymers make the metabolism much more sophisticated and even more difficult to determine. In this study, we present a continuous sequence of 18 amino acids (FFAARTMIWY(d-P)GAWYKRI). It forms nanospheres around 170 nm, which increase slightly after loading with siRNA and DOX. Notably, it can be internalized by cancer cells mainly through electronic interactions and PD-L1-mediated endocytosis. Compared with poly-l-lysine and polyethyleneimine, it has a much higher efficiency (about four times) of gene transduction while lowering toxicity. In the treatment of cancer, it causes apoptosis (21%) and inhibits the expression of SURVIVIN protein in vitro. In vivo, it shows good biocompatibility as there are no changes in mice’s body weight. When administering peptide-siRNA-DOX, tumor growth is inhibited the most (about three times). These results above prove the sequence to be a good candidate for gene therapy and drug delivery.

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