scholarly journals Molecular partners for interaction and cell internalization of cell-penetrating peptides: how identical are they?

Nanomedicine ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. 133-143 ◽  
Author(s):  
Astrid Walrant ◽  
Chérine Bechara ◽  
Isabel D Alves ◽  
Sandrine Sagan
Keyword(s):  
Cell Penetrating Peptides ◽  
Cell Internalization ◽  
Cell Penetrating

scholarly journals β-Lactamase Tools for Establishing Cell Internalization and Cytosolic Delivery of Cell Penetrating Peptides

Biomolecules ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 51 ◽  
Author(s):  
Shane Stone ◽  
Tatjana Heinrich ◽  
Suzy Juraja ◽  
Jiulia Satiaputra ◽  
Clinton Hall ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Cell Penetrating Peptides ◽  
Stable Cell Line ◽  
Intracellular Space ◽  
Biologically Relevant ◽  
Cell Internalization ◽  
Cytosolic Delivery ◽  
Cell Penetrating ◽  
Split Protein

The ability of cell penetrating peptides (CPPs) to deliver biologically relevant cargos into cells is becoming more important as targets in the intracellular space continue to be explored. We have developed two assays based on CPP-dependent, intracellular delivery of TEM-1 β-lactamase enzyme, a functional biological molecule comparable in size to many protein therapeutics. The first assay focuses on the delivery of full-length β-lactamase to evaluate the internalization potential of a CPP sequence. The second assay uses a split-protein system where one component of β-lactamase is constitutively expressed in the cytoplasm of a stable cell line and the other component is delivered by a CPP. The delivery of a split β-lactamase component evaluates the cytosolic delivery capacity of a CPP. We demonstrate that these assays are rapid, flexible and have potential for use with any cell type and CPP sequence. Both assays are validated using canonical and novel CPPs, with limits of detection from <500 nM to 1 µM. Together, the β-lactamase assays provide compatible tools for functional characterization of CPP activity and the delivery of biological cargos into cells.

scholarly journals Cell-Penetrating Peptides: a Useful Tool for the Delivery of Various Cargoes Into Cells

2018 ◽  
pp. S267-S279 ◽  
Author(s):  
E. BÖHMOVÁ ◽  
D. MACHOVÁ ◽  
M. PECHAR ◽  
R. POLA ◽  
K. VENCLÍKOVÁ ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Cellular Membrane ◽  
Cell Penetrating Peptides ◽  
Cell Entry ◽  
Biologically Active ◽  
Cell Internalization ◽  
Structural Types ◽  
Cell Penetrating ◽  
History Of ◽  
Preclinical And Clinical Studies

Cell-penetrating compounds are substances that enhance the cellular uptake of various molecular cargoes that do not easily cross the cellular membrane. The majority of cell-penetrating compounds described in the literature are cell-penetrating peptides (CPPs). This review summarizes the various structural types of cell-penetrating compounds, with the main focus on CPPs. The authors present a brief overview of the history of CPPs, discuss the various types of conjugation of CPPs to biologically active cargoes intended for cell internalization, examine the cell-entry mechanisms of CPPs, and report on the applications of CPPs in research and in preclinical and clinical studies.

scholarly journals Designer Amyloid Cell-Penetrating Peptides for Potential Use as Gene Transfer Vehicles

Biomolecules ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 7 ◽  
Author(s):  
Chrysoula Kokotidou ◽  
Sai Vamshi R. Jonnalagadda ◽  
Asuka A. Orr ◽  
George Vrentzos ◽  
Androniki Kretsovali ◽  
...  
Keyword(s):  
Gene Transfer ◽  
Mammalian Cells ◽  
Amyloid Fibrils ◽  
Cell Penetrating Peptides ◽  
Retroviral Infection ◽  
Aromatic Residues ◽  
Cell Internalization ◽  
Cell Penetrating ◽  
Β Sheet ◽  
Positively Charged

Cell-penetrating peptides are used extensively to deliver molecules into cells due to their unique characteristics such as rapid internalization, charge, and non-cytotoxicity. Amyloid fibril biomaterials were reported as gene transfer or retroviral infection enhancers; no cell internalization of the peptides themselves is reported so far. In this study, we focus on two rationally and computationally designed peptides comprised of β-sheet cores derived from naturally occurring protein sequences and designed positively charged and aromatic residues exposed at key residue positions. The β-sheet cores bestow the designed peptides with the ability to self-assemble into amyloid fibrils. The introduction of positively charged and aromatic residues additionally promotes DNA condensation and cell internalization by the self-assembled material formed by the designed peptides. Our results demonstrate that these designer peptide fibrils can efficiently enter mammalian cells while carrying packaged luciferase-encoding plasmid DNA, and they can act as a protein expression enhancer. Interestingly, the peptides additionally exhibited strong antimicrobial activity against the enterobacterium Escherichia coli.

scholarly journals Cell-Penetrating Peptides Predicted From CASC3, AKIP1, and AHRR Proteins

2021 ◽  
Vol 12 ◽  
Author(s):  
Ly Porosk ◽  
Kaisa Põhako ◽  
Piret Arukuusk ◽  
Ülo Langel
Keyword(s):  
Special Property ◽  
Cell Penetrating Peptides ◽  
Therapeutic Applications ◽  
Protein Protein Interaction ◽  
Cell Internalization ◽  
Cell Penetrating ◽  
Peptide Prediction ◽  
Small Molecule Modulators ◽  
Multifunctional Peptides ◽  
Intracellular Targets

Peptides can be used as research tools and for diagnostic or therapeutic applications. Peptides, alongside small molecules and antibodies, are used and are gaining further interest as protein-protein interaction (PPI) modulators. Peptides have high target specificity and high affinity, but, unlike small molecule modulators, they are not able to cross the cell membranes to reach their intracellular targets. To overcome this limitation, the special property of the cell-penetrating peptides (CPPs) could benefit their cause. CPPs are a class of peptides that can enter the cells and with them also deliver the attached cargoes. Today, with the advancement of in silico prediction tools and the availability of protein databases, designing new and multifunctional peptides that are able to reach intracellular targets and inhibit certain cellular processes in a very specific manner is reachable. Although there are several efficient CPP sequences already known, the discovery of new CPPs is crucial for the development of efficient delivery methods for both biotechnological and therapeutic applications. In this work, we chose 10 human nuclear proteins from which we predicted new potential CPP sequences by using three different CPP predictors: cell-penetrating peptide prediction tool, CellPPD, and SkipCPP-Pred. From each protein, one predicted CPP sequence was synthesized and its internalization into cells was assessed. Out of the tested sequences, three peptides displayed features characteristic to CPPs. These peptides and also the predicted peptide sequences could be used to design and modify new CPPs. In this work, we show that we can use protein sequences as input for generating new peptides with cell internalization properties. Three new CPPs, AHRR8-24, CASC3251-264, and AKIP127-37, can be further used for the delivery of other cargoes or designed into multifunctional peptides with capability of internalizing cells.

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