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 Peptides and Dendrimers: How to Combat Viral and Bacterial Infections

Pharmaceutics ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 101
Author(s):  
Annarita Falanga ◽  
Valentina Del Genio ◽  
Stefania Galdiero
Keyword(s):  
Antimicrobial Resistance ◽  
Antimicrobial Peptides ◽  
Broad Spectrum ◽  
Bacterial Infections ◽  
Cell Penetrating Peptides ◽  
High Potential ◽  
Permanent Damage ◽  
Antiviral Peptides ◽  
Cell Penetrating ◽  
Novel Approaches

The alarming growth of antimicrobial resistance and recent viral pandemic events have enhanced the need for novel approaches through innovative agents that are mainly able to attach to the external layers of bacteria and viruses, causing permanent damage. Antimicrobial molecules are potent broad-spectrum agents with a high potential as novel therapeutics. In this context, antimicrobial peptides, cell penetrating peptides, and antiviral peptides play a major role, and have been suggested as promising solutions. Furthermore, dendrimers are to be considered as suitable macromolecules for the development of advanced nanosystems that are able to complement the typical properties of dendrimers with those of peptides. This review focuses on the description of nanoplatforms constructed with peptides and dendrimers, and their applications.

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.

scholarly journals Synthesis and cellular penetration properties of new phosphonium based cationic amphiphilic peptides

MedChemComm ◽  
2018 ◽  
Vol 9 (6) ◽  
pp. 982-987 ◽  
Author(s):  
Ezequiel Silva Nigenda ◽  
Tobias M. Postma ◽  
Mohammed Hezwani ◽  
Alin Pirvan ◽  
Susan Gannon ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Penetrating Peptides ◽  
Amphiphilic Peptides ◽  
Cell Penetrating

A new category of phosphonium based cationic amphiphilic peptides has been developed and evaluated as potential antimicrobial peptides and cell penetrating peptides.

scholarly journals Stabilin-1 plays a protective role against Listeria monocytogenes infection through the regulation of cytokine and chemokine production and immune cell recruitment

2021 ◽  
Author(s):  
Rita Pombinho ◽  
Jorge Pinheiro ◽  
Mariana Resende ◽  
Diana Meireles ◽  
Sirpa Jalkanen ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Defense Mechanisms ◽  
Bacterial Infections ◽  
Immune Cell ◽  
Scavenger Receptor ◽  
Protective Role ◽  
Host Cells ◽  
Cell Trafficking ◽  
Host Cell Membrane ◽  
Chemokine Production

ABSTRACTScavenger receptors are part of a complex surveillance system expressed by host cells to efficiently orchestrate innate immune response against bacterial infections. Stabilin-1 (STAB-1) is a scavenger receptor involved in cell trafficking, inflammation and cancer, however its role in infection remains to be elucidated. Listeria monocytogenes (Lm) is a major intracellular human food-borne pathogen causing severe infections in susceptible hosts. Using a mouse model of infection, we demonstrate here that STAB-1 controls Lm-induced cytokine and chemokine production and immune cell accumulation in Lm-infected organs. We show that STAB-1 also regulates the recruitment of myeloid cells in response to Lm infection and contributes to clear circulating bacteria. In addition, whereas STAB-1 appears to promote bacterial uptake by macrophages, infection by pathogenic Listeria induces the down regulation of STAB-1 expression and its delocalization from the host cell membrane.We propose STAB-1 as a new SR involved in the control of Lm infection through the regulation of host defense mechanisms, a process that would be targeted by bacterial virulence factors to promote infection.

scholarly journals Membrane Active Peptides and Their Biophysical Characterization

Biomolecules ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 77 ◽  
Author(s):  
Fatma Gizem Avci ◽  
Berna Sariyar Akbulut ◽  
Elif Ozkirimli
Keyword(s):  
Antimicrobial Peptides ◽  
Single Molecule ◽  
Imaging Techniques ◽  
Membrane Integrity ◽  
Cell Penetrating Peptides ◽  
Single Molecule Level ◽  
Active Peptides ◽  
Cell Penetrating ◽  
Biophysical Techniques ◽  
Membrane Active Peptides

In the last 20 years, an increasing number of studies have been reported on membrane active peptides. These peptides exert their biological activity by interacting with the cell membrane, either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. Membrane active peptides are attractive alternatives to currently used pharmaceuticals and the number of antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery in the drug pipeline is increasing. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). Antimicrobial peptides are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus, and fungi. Cell penetrating peptides are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity. Biophysical techniques shed light on peptide–membrane interactions at higher resolution due to the advances in optics, image processing, and computational resources. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Live imaging techniques allow examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provide clues on the peptide–lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

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 role of membrane tension in the action of antimicrobial peptides and cell-penetrating peptides in biomembranes

2019 ◽  
Vol 11 (3) ◽  
pp. 431-448 ◽  
Author(s):  
Moynul Hasan ◽  
Md. Mizanur Rahman Moghal ◽  
Samiron Kumar Saha ◽  
Masahito Yamazaki
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Penetrating Peptides ◽  
Membrane Tension ◽  
Cell Penetrating

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.

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