scholarly journals Cell-penetrating peptides and antimicrobial peptides: how different are they?

2006 ◽  
Vol 399 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Sónia Troeira Henriques ◽  
Manuel Nuno Melo ◽  
Miguel A. R. B. Castanho
Keyword(s):  
Cell Membrane ◽  
Antimicrobial Peptides ◽  
Cellular Uptake ◽  
Mammalian Cells ◽  
Cell Penetrating Peptides ◽  
Host Cells ◽  
Cell Penetrating ◽  
New Perspective ◽  
Pathogenic Agents ◽  
Endocytic Pathways

Some cationic peptides, referred to as CPPs (cell-penetrating peptides), have the ability to translocate across biological membranes in a non-disruptive way and to overcome the impermeable nature of the cell membrane. They have been successfully used for drug delivery into mammalian cells; however, there is no consensus about the mechanism of cellular uptake. Both endocytic and non-endocytic pathways are supported by experimental evidence. The observation that some AMPs (antimicrobial peptides) can enter host cells without damaging their cytoplasmic membrane, as well as kill pathogenic agents, has also attracted attention. The capacity to translocate across the cell membrane has been reported for some of these AMPs. Like CPPs, AMPs are short and cationic sequences with a high affinity for membranes. Similarities between CPPs and AMPs prompted us to question if these two classes of peptides really belong to unrelated families. In this Review, a critical comparison of the mechanisms that underlie cellular uptake is undertaken. A reflection and a new perspective about CPPs and AMPs are presented.

siRNA versus pharmacological inhibition of endocytic pathways for studying cellular uptake of cell penetrating peptides and other drug delivery vectors

2010 ◽  
Vol 15 (23-24) ◽  
pp. 1103-1103
Author(s):  
Monerah H. Al-Soraj ◽  
Catherine L. Watkins ◽  
Dries Vercauteren ◽  
Stefaan De Smedt ◽  
Kevin Braeckmans ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Cellular Uptake ◽  
Cell Penetrating Peptides ◽  
Pharmacological Inhibition ◽  
Cell Penetrating ◽  
Endocytic Pathways

scholarly journals Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules

2005 ◽  
Vol 390 (2) ◽  
pp. 407-418 ◽  
Author(s):  
Catherine de Coupade ◽  
Antonio Fittipaldi ◽  
Vanessa Chagnas ◽  
Matthieu Michel ◽  
Sophie Carlier ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Mammalian Cells ◽  
Heparan Sulphate ◽  
Intracellular Delivery ◽  
Membrane Lipid ◽  
Cell Penetrating Peptides ◽  
Heparin Binding ◽  
Independent Manner ◽  
Cell Penetrating

Short peptide sequences that are able to transport molecules across the cell membrane have been developed as tools for intracellular delivery of therapeutic molecules. This work describes a novel family of cell-penetrating peptides named Vectocell® peptides [also termed DPVs (Diatos peptide vectors)]. These peptides, originating from human heparin binding proteins and/or anti-DNA antibodies, once conjugated to a therapeutic molecule, can deliver the molecule to either the cytoplasm or the nucleus of mammalian cells. Vectocell® peptides can drive intracellular delivery of molecules of varying molecular mass, including full-length active immunoglobulins, with efficiency often greater than that of the well-characterized cell-penetrating peptide Tat. The internalization of Vectocell® peptides has been demonstrated to occur in both adherent and suspension cell lines as well as in primary cells through an energy-dependent endocytosis process, involving cell-membrane lipid rafts. This endocytosis occurs after binding of the cell-penetrating peptides to extracellular heparan sulphate proteoglycans, except for one particular peptide (DPV1047) that partially originates from an anti-DNA antibody and is internalized in a caveolar independent manner. These new therapeutic tools are currently being developed for intracellular delivery of a number of active molecules and their potentiality for in vivo transduction investigated.

siRNA versus pharmacological inhibition of endocytic pathways for studying cellular uptake of cell penetrating peptides

2010 ◽  
Vol 148 (1) ◽  
pp. e86-e87 ◽  
Author(s):  
Monerah H. Al-Soraj ◽  
Catherine L. Watkins ◽  
Dries Vercauteren ◽  
Stefaan C. De Smedt ◽  
Kevin Braeckmans ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Cell Penetrating Peptides ◽  
Pharmacological Inhibition ◽  
Cell Penetrating ◽  
Endocytic Pathways

scholarly journals Modified defence peptides from horseshoe crab target and kill bacteria inside host cells

2021 ◽  
Author(s):  
Anna S Amiss ◽  
Jessica B von Pein ◽  
Jessica R Webb ◽  
Nicholas D Condon ◽  
Peta J Harvey ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Pathogenic Bacteria ◽  
Horseshoe Crab ◽  
Cell Penetrating Peptides ◽  
Host Cells ◽  
Therapeutic Window ◽  
Infection Model ◽  
Zinc Toxicity ◽  
Cell Penetrating ◽  
Tachyplesin I

Bacteria that occupy an intracellular niche can evade extracellular host immune responses and antimicrobial molecules. In addition to classic intracellular pathogens, other bacteria including uropathogenic Escherichia coli (UPEC) can adopt both extracellular and intracellular lifestyles. UPEC intracellular survival and replication complicates treatment, as many therapeutic molecules do not effectively reach all components of the infection cycle. In this study, we explored cell penetrating antimicrobial peptides from distinct structural classes as alternative molecules for targeting bacteria. We identified two β-hairpin peptides from the horseshoe crab, tachyplesin I and polyphemusin I, with broad antimicrobial activity toward a panel of pathogenic and non-pathogenic bacteria in planktonic form. Peptide analogues [I11A]tachyplesin I and [I11S]tachyplesin I maintained activity toward bacteria, but were less toxic to mammalian cells than native tachyplesin I. This important increase in therapeutic window allowed treatment with higher concentrations of [I11A]tachyplesin I and [I11S]tachyplesin I, to significantly reduce intramacrophage survival of UPEC in an in vitro infection model. Mechanistic studies using bacterial cells, model membranes and cell membrane extracts, suggest that tachyplesin I and polyphemusin I peptides kill UPEC by selectively binding and disrupting bacterial cell membranes. Moreover, treatment of UPEC with sublethal peptide concentrations increased zinc toxicity and enhanced innate macrophage antimicrobial pathways. In summary, our combined data show that cell penetrating peptides are attractive alternatives to traditional small molecule antimicrobials for treating UPEC infection, and that optimization of native peptide sequences can deliver effective antimicrobials for targeting bacteria in extracellular and intracellular environments.

scholarly journals The J-Domain of Heat Shock Protein 40 Can Enhance the Transduction Efficiency of Arginine-Rich Cell-Penetrating Peptides

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Tzu-Yin Lin ◽  
Yu-Hsiu Su ◽  
Kun-Hsiung Lee ◽  
Chin-Kai Chuang
Keyword(s):  
Recombinant Proteins ◽  
Mammalian Cells ◽  
Cellular Membrane ◽  
Cell Penetrating Peptides ◽  
Endosomal Escape ◽  
Host Cells ◽  
Soluble Form ◽  
Transduction Efficiency ◽  
E Coli ◽  
Cell Penetrating

Sense and antisense oligonucleotide pairs encoding cell-penetrating peptides PTD(Tat47–57), DPV3A, E162, pVEC, R11, and TP13 were used to construct two sets of pET22b-CPP-DsRed and pET22b-CPP-J-DsRed vectors for CPP-DsRed and CPP-J-DsRed recombinant proteins expression. PTD-DsRed, DPV3A-DsRed, PTD-J-DsRed, and DPV3A-J-DsRed recombinant proteins were expressed in a soluble form. PTD-J-DsRed and DPV3A-J-DsRed recombinant proteins were able to escape fromE. colihost cells into the culture medium. The membrane-penetrating activity of PTD-J-DsRed and DPV3A-J-DsRed recombinant proteins to mammalian cells was more effective than that of PTD-DsRed and DPV3A-DsRed. The route of the cellular membrane translocation of these recombinant proteins is suggested via macropinocytosis followed by an endosomal escape pathway.

scholarly journals Antimicrobial Peptides and Cell-Penetrating Peptides for Treating Intracellular Bacterial Infections

2021 ◽  
Vol 10 ◽  
Author(s):  
Danieli F. Buccini ◽  
Marlon H. Cardoso ◽  
Octavio L. Franco
Keyword(s):  
Antimicrobial Peptides ◽  
Bacterial Infections ◽  
Antibacterial Activities ◽  
Cell Penetrating Peptides ◽  
Host Cells ◽  
Host Cell Membrane ◽  
Infection Treatment ◽  
Cell Penetrating ◽  
High Doses ◽  
Higher Doses

Bacterial infections caused by intracellular pathogens are difficult to control. Conventional antibiotic therapies are often ineffective, as high doses are needed to increase the number of antibiotics that will cross the host cell membrane to act on the intracellular bacterium. Moreover, higher doses of antibiotics may lead to elevated severe toxic effects against host cells. In this context, antimicrobial peptides (AMPs) and cell-penetrating peptides (CPPs) have shown great potential to treat such infections by acting directly on the intracellular pathogenic bacterium or performing the delivery of cargos with antibacterial activities. Therefore, in this mini-review, we cover the main AMPs and CPPs described to date, aiming at intracellular bacterial infection treatment. Moreover, we discuss some of the proposed mechanisms of action for these peptide classes and their conjugation with other antimicrobials.

scholarly journals Cellular Uptake of Arginine-Rich Cell-Penetrating Peptides and the Contribution of Membrane-Associated Proteoglycans

2015 ◽  
Vol 27 (155) ◽  
pp. 81-88 ◽  
Author(s):  
Ikuhiko Nakase ◽  
Yoshimasa Kawaguchi ◽  
Motoyoshi Nomizu ◽  
Shiroh Futaki
Keyword(s):  
Cellular Uptake ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals A comparison of acyl-moieties for noncovalent functionalization of PLGA and PEG-PLGA nanoparticles with a cell-penetrating peptide

RSC Advances ◽  
2021 ◽  
Vol 11 (57) ◽  
pp. 36116-36124
Author(s):  
Omar Paulino da Silva Filho ◽  
Muhanad Ali ◽  
Rike Nabbefeld ◽  
Daniel Primavessy ◽  
Petra H. Bovee-Geurts ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Plga Nanoparticles ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating Peptide ◽  
Noncovalent Functionalization ◽  
Cell Penetrating ◽  
A Cell

Noncovalent functionalization with acylated cell-penetrating peptides achieves an efficient cellular uptake of PLGA and PEG-PLGA nanoparticles.

scholarly journals Enhanced delivery of protein fused to cell penetrating peptides to mammalian cells

BMB Reports ◽  
2019 ◽  
Vol 52 (5) ◽  
pp. 324-329 ◽  
Author(s):  
Jung-Il Moon ◽  
Min-Joon Han ◽  
Shin-Hye Yu ◽  
Eun-Hye Lee ◽  
Sang-Mi Kim ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating
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