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Journal articles on the topic 'Cell-penetrating peptides (CPPs)'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Eggimann, Gabriela A., Emilyne Blattes, Stefanie Buschor, et al. "Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells." Chem. Commun. 50, no. 55 (2014): 7254–57. http://dx.doi.org/10.1039/c4cc02780a.

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Redesigning linear cell penetrating peptides (CPPs) into a multi-branched topology with short dipeptide branches gave cell penetrating peptide dendrimers (CPPDs) with higher cell penetration, lower toxicity and hemolysis and higher serum stability than linear CPPs.

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Kerkis, Alexandre, Mirian A. F. Hayashi, Tetsuo Yamane, and Irina Kerkis. "Properties of cell penetrating peptides (CPPs)." IUBMB Life 58, no. 1 (2006): 7–13. http://dx.doi.org/10.1080/15216540500494508.

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Shamova, O. V., A. S. Nazarov, P. M. Kopeykin, et al. "BACTENECINS AS CELL-PENETRATING PEPTIDES." Medical academic journal 19, no. 1S (2019): 178–79. http://dx.doi.org/10.17816/maj191s1178-179.

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Cell-Penetrating Peptides (CPPs) are molecules that can easily internalize into eukaryotic cells, as well as deliver across their membranes a variety of compounds (proteins, nucleic acids, liposomes, nanoparticles, etc.). CPPs are considered as promising components of anticancer drugs, serving for delivery of active ingredients into malignant cells, therefore, a detailed study of a mechanism of action of CPPs and search for novel, more effective peptides are vital tasks of current biological and medical research. An ability of proline-rich peptides bactenecins (ChBac5, ChBac3.4, mini-ChBac7.5N

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Morán-Torres, Rafael, David A. Castillo González, Maria Luisa Durán-Pastén, Beatriz Aguilar-Maldonado, Susana Castro-Obregón, and Gabriel Del Rio. "Selective Moonlighting Cell-Penetrating Peptides." Pharmaceutics 13, no. 8 (2021): 1119. http://dx.doi.org/10.3390/pharmaceutics13081119.

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Cell penetrating peptides (CPPs) are molecules capable of passing through biological membranes. This capacity has been used to deliver impermeable molecules into cells, such as drugs and DNA probes, among others. However, the internalization of these peptides lacks specificity: CPPs internalize indistinctly on different cell types. Two major approaches have been described to address this problem: (i) targeting, in which a receptor-recognizing sequence is added to a CPP, and (ii) activation, where a non-active form of the CPP is activated once it interacts with cell target components. These str

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Ruseska, Ivana, and Andreas Zimmer. "Internalization mechanisms of cell-penetrating peptides." Beilstein Journal of Nanotechnology 11 (January 9, 2020): 101–23. http://dx.doi.org/10.3762/bjnano.11.10.

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In today’s modern era of medicine, macromolecular compounds such as proteins, peptides and nucleic acids are dethroning small molecules as leading therapeutics. Given their immense potential, they are highly sought after. However, their application is limited mostly due to their poor in vivo stability, limited cellular uptake and insufficient target specificity. Cell-penetrating peptides (CPPs) represent a major breakthrough for the transport of macromolecules. They have been shown to successfully deliver proteins, peptides, siRNAs and pDNA in different cell types. In general, CPPs are basic p

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Adhikari, Sayanee, Turki I. Alahmadi, Zifan Gong, and Amy J. Karlsson. "Expression of Cell-Penetrating Peptides Fused to Protein Cargo." Journal of Molecular Microbiology and Biotechnology 28, no. 4 (2018): 159–68. http://dx.doi.org/10.1159/000494084.

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Cell-penetrating peptides (CPPs) are short peptides that can cross cell membranes. CPPs enable the delivery of biomolecules into cells and can act as drug-delivery vectors. Because recombinant production of CPPs as fusions to protein “cargo” leads to low yields for some CPP-cargo fusions, approaches to enhance the recombinant expression of peptide-cargo fusions need to be identified. We optimized expression conditions in <i>Escherichia coli</i> for fusions of CPPs (SynB, histatin-5, and MPG) to the cargo proteins biotin carboxyl carrier protein, maltose-binding protein, and green f

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Henriques, Sónia Troeira, Manuel Nuno Melo, and Miguel A. R. B. Castanho. "Cell-penetrating peptides and antimicrobial peptides: how different are they?" Biochemical Journal 399, no. 1 (2006): 1–7. http://dx.doi.org/10.1042/bj20061100.

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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,

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Brugnano, Jamie, Brian C. Ward, and Alyssa Panitch. "Cell penetrating peptides can exert biological activity: a review." BioMolecular Concepts 1, no. 2 (2010): 109–16. http://dx.doi.org/10.1515/bmc.2010.016.

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AbstractCell penetrating peptides (CPPs) have been successful in delivering cargo into many different cell types and are an important alternative to other methods of permeation that might damage the integrity of the cell membrane. The traditional view of CPPs is that they are inert molecules that can be successfully used to deliver many cargos intracellularly. The goal of this review is to challenge this traditional understanding of CPPs. Recent literature has demonstrated that CPPs themselves can convey biological activity, including the alteration of gene expression and inhibition of protein

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Chen, L., and S. D. Harrison. "Cell-penetrating peptides in drug development: enabling intracellular targets." Biochemical Society Transactions 35, no. 4 (2007): 821–25. http://dx.doi.org/10.1042/bst0350821.

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A large body of literature has shown that CPPs (cell-penetrating peptides) are capable of carrying macromolecules across the plasma membrane. CPPs can penetrate a wide variety of tissue types and enable modulation of intracellular targets with molecules that, by themselves, are incapable of penetrating cells. As a result, CPPs are recognized for their potential value in validating intracellular targets that could lead to drug discovery programmes [Dietz and Bahr (2004) Mol. Cell Neurosci. 27, 85–131]. The potential for CPP–drug conjugates to be used as human therapeutic agents has not been ext

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Taylor, Rebecca E., and Maliha Zahid. "Cell Penetrating Peptides, Novel Vectors for Gene Therapy." Pharmaceutics 12, no. 3 (2020): 225. http://dx.doi.org/10.3390/pharmaceutics12030225.

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Cell penetrating peptides (CPPs), also known as protein transduction domains (PTDs), first identified ~25 years ago, are small, 6–30 amino acid long, synthetic, or naturally occurring peptides, able to carry variety of cargoes across the cellular membranes in an intact, functional form. Since their initial description and characterization, the field of cell penetrating peptides as vectors has exploded. The cargoes they can deliver range from other small peptides, full-length proteins, nucleic acids including RNA and DNA, liposomes, nanoparticles, and viral particles as well as radioisotopes an

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Madani, Fatemeh, Staffan Lindberg, Ülo Langel, Shiroh Futaki, and Astrid Gräslund. "Mechanisms of Cellular Uptake of Cell-Penetrating Peptides." Journal of Biophysics 2011 (April 7, 2011): 1–10. http://dx.doi.org/10.1155/2011/414729.

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Recently, much attention has been given to the problem of drug delivery through the cell-membrane in order to treat and manage several diseases. The discovery of cell penetrating peptides (CPPs) represents a major breakthrough for the transport of large-cargo molecules that may be useful in clinical applications. CPPs are rich in basic amino acids such as arginine and lysine and are able to translocate over membranes and gain access to the cell interior. They can deliver large-cargo molecules, such as oligonucleotides, into cells. Endocytosis and direct penetration have been suggested as the t

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Ross, M. F., and M. P. Murphy. "Cell-penetrating peptides are excluded from the mitochondrial matrix." Biochemical Society Transactions 32, no. 6 (2004): 1072–74. http://dx.doi.org/10.1042/bst0321072.

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CPPs (cell-penetrating peptides) facilitate cellular uptake of covalently attached macromolecules, through an as yet controversial mechanism that either involves direct membrane passage or a type of endocytosis. We investigated the potential of the CPPs penetratin and Tat to act as mitochondria-targeting vectors by testing whether they were internalized by isolated mitochondria, and by mitochondria within cells in culture. We also tested peptides conjugated to the mitochondria-targeting moiety triphenylphosphonium. We found no evidence for mitochondrial uptake by penetratin, Tat or their triph

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Melnick, A. "Targeting aggressive B-cell lymphomas with cell-penetrating peptides." Biochemical Society Transactions 35, no. 4 (2007): 802–6. http://dx.doi.org/10.1042/bst0350802.

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DLBCL (diffuse large B-cell lymphoma) is the most common subtype of non-Hodgkin's lymphoma. Current therapy for patients includes chemotherapy and monoclonal antibodies. Although oncogene-targeted therapy is dramatically successful for patients with certain kinds of leukaemias, there are no such agents yet for DLBCL. One reason for this is that several key oncogenes involved in DLBCL pathogenesis are transcription factors, which are difficult to therapeutically target with small molecules. Recent advances in the structural and functional characterization of DLBCL oncogenes have facilitated des

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García-Sosa, Alfonso T., Indrek Tulp, Kent Langel, and Ülo Langel. "Peptide-Ligand Binding Modeling of siRNA with Cell-Penetrating Peptides." BioMed Research International 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/257040.

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The binding affinity of a series of cell-penetrating peptides (CPP) was modeled through docking and making use of the number of intermolecular hydrogen bonds, lipophilic contacts, and the number of sp3 molecular orbital hybridization carbons. The new ranking of the peptides is consistent with the experimentally determined efficiency in the downregulation of luciferase activity, which includes the peptides’ ability to bind and deliver the siRNA into the cell. The predicted structures of the complexes of peptides to siRNA were stable throughout 10 ns long, explicit water molecular dynamics simul

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Stiltner, Jeffrey, Kayla McCandless, and Maliha Zahid. "Cell-Penetrating Peptides: Applications in Tumor Diagnosis and Therapeutics." Pharmaceutics 13, no. 6 (2021): 890. http://dx.doi.org/10.3390/pharmaceutics13060890.

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Since their identification over twenty-five years ago, the plethora of cell-penetrating peptides (CPP) and their applications has skyrocketed. These 5 to 30 amino acid in length peptides have the unique property of breaching the cell membrane barrier while carrying cargoes larger than themselves into cells in an intact, functional form. CPPs can be conjugated to fluorophores, activatable probes, radioisotopes or contrast agents for imaging tissues, such as tumors. There is no singular mechanism for translocation of CPPs into a cell, and therefore, many CPPs are taken up by a multitude of cell

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El-Andaloussi, Samir, Peter Järver, Henrik J. Johansson, and Ülo Langel. "Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: a comparative study." Biochemical Journal 407, no. 2 (2007): 285–92. http://dx.doi.org/10.1042/bj20070507.

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The use of CPPs (cell-penetrating peptides) as delivery vectors for bioactive molecules has been an emerging field since 1994 when the first CPP, penetratin, was discovered. Since then, several CPPs, including the widely used Tat (transactivator of transcription) peptide, have been developed and utilized to translocate a wide range of compounds across the plasma membrane of cells both in vivo and in vitro. Although the field has emerged as a possible future candidate for drug delivery, little attention has been given to the potential toxic side effects that these peptides might exhibit in carg

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Langel, Ülo. "Cell-Penetrating Peptides and Transportan." Pharmaceutics 13, no. 7 (2021): 987. http://dx.doi.org/10.3390/pharmaceutics13070987.

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In the most recent 25–30 years, multiple novel mechanisms and applications of cell-penetrating peptides (CPP) have been demonstrated, leading to novel drug delivery systems. In this review, I present a brief introduction to the CPP area with selected recent achievements. This is followed by a nostalgic journey into the research in my own laboratories, which lead to multiple CPPs, starting from transportan and paving a way to CPP-based therapeutic developments in the delivery of bio-functional materials, such as peptides, proteins, vaccines, oligonucleotides and small molecules, etc.

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Abes, R., A. A. Arzumanov, H. M. Moulton, et al. "Cell-penetrating-peptide-based delivery of oligonucleotides: an overview." Biochemical Society Transactions 35, no. 4 (2007): 775–79. http://dx.doi.org/10.1042/bst0350775.

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Cationic CPPs (cell-penetrating peptides) have been used largely for intracellular delivery of low-molecular-mass drugs, biomolecules and particles. Most cationic CPPs bind to cell-associated glycosaminoglycans and are internalized by endocytosis, although the detailed mechanisms involved remain controversial. Sequestration and degradation in endocytic vesicles severely limits the efficiency of cytoplasmic and/or nuclear delivery of CPP-conjugated material. Re-routing the splicing machinery by using steric-block ON (oligonucleotide) analogues, such as PNAs (peptide nucleic acids) or PMOs (phos

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Rathnayake, P. V. G. M., B. G. C. M. Gunathunge, P. N. Wimalasiri, D. N. Karunaratne, and R. J. K. U. Ranatunga. "Trends in the Binding of Cell Penetrating Peptides to siRNA: A Molecular Docking Study." Journal of Biophysics 2017 (February 21, 2017): 1–12. http://dx.doi.org/10.1155/2017/1059216.

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The use of gene therapeutics, including short interfering RNA (siRNA), is limited by the lack of efficient delivery systems. An appealing approach to deliver gene therapeutics involves noncovalent complexation with cell penetrating peptides (CPPs) which are able to penetrate the cell membranes of mammals. Although a number of CPPs have been discovered, our understanding of their complexation and translocation of siRNA is as yet insufficient. Here, we report on computational studies comparing the binding affinities of CPPs with siRNA, considering a variety of CPPs. Specifically, seventeen CPPs

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Jobin, Marie-Lise, Lydie Vamparys, Romain Deniau, et al. "Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide." International Journal of Molecular Sciences 20, no. 18 (2019): 4441. http://dx.doi.org/10.3390/ijms20184441.

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Cell-penetrating peptides (CPPs) are short peptides that can translocate and transport cargoes into the intracellular milieu by crossing biological membranes. The mode of interaction and internalization of cell-penetrating peptides has long been controversial. While their interaction with anionic membranes is quite well understood, the insertion and behavior of CPPs in zwitterionic membranes, a major lipid component of eukaryotic cell membranes, is poorly studied. Herein, we investigated the membrane insertion of RW16 into zwitterionic membranes, a versatile CPP that also presents antibacteria

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Tang, Jihui, Jie Ning, Xiaoyan Liu, Baoming Wu, and Rongfeng Hu. "A Novel Amino Acid Sequence-based Computational Approach to Predicting Cell-penetrating Peptides." Current Computer-Aided Drug Design 15, no. 3 (2019): 206–11. http://dx.doi.org/10.2174/1573409914666180925100355.

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<P>Introduction: Machine Learning is a useful tool for the prediction of cell-penetration compounds as drug candidates. </P><P> Materials and Methods: In this study, we developed a novel method for predicting Cell-Penetrating Peptides (CPPs) membrane penetrating capability. For this, we used orthogonal encoding to encode amino acid and each amino acid position as one variable. Then a software of IBM spss modeler and a dataset including 533 CPPs, were used for model screening. </P><P> Results: The results indicated that the machine learning model of Support Vector

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Järver, P., K. Langel, S. El-Andaloussi, and Ü. Langel. "Applications of cell-penetrating peptides in regulation of gene expression." Biochemical Society Transactions 35, no. 4 (2007): 770–74. http://dx.doi.org/10.1042/bst0350770.

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CPPs (cell-penetrating peptides) can be defined as short peptides that are able to efficiently penetrate cellular lipid bilayers. Because of this remarkable feature, they are excellent candidates regarding alterations in gene expression. CPPs have been utilized in in vivo and in vitro experiments as delivery vectors for different bioactive cargoes. This review focuses on the experiments performed in recent years where CPPs have been used as vectors for multiple effectors of gene expression such as oligonucleotides for antisense, siRNA (small interfering RNA) and decoy dsDNA (double-stranded DN

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Tooyserkani, Raheleh, Wojciech Lipiński, Bob Willemsen, and Dennis W. P. M. Löwik. "Activation of cell-penetrating peptide fragments by disulfide formation." Amino Acids 52, no. 8 (2020): 1161–68. http://dx.doi.org/10.1007/s00726-020-02880-x.

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Abstract Three cell-penetrating peptides (CPPs), Tat, Pep-3 and penetratin, were split into two parts and each fragment was terminated with a cysteine residue, to allow disulfide bridge formation, as well as a fluorescent label, for visualization and quantitative analysis. After disulfide formation between two complementary CPP fragments, cellular uptake of the resulting conjugates was observed. As confirmed by in vitro experiments, the conjugated peptides showed uptake activity comparable to the native CPP sequences, while the truncated peptides were hardly active. Until now, this split CPP s

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Perche. "Stimuli-Sensitive Cell Penetrating Peptide-Modified Nanocarriers." Processes 7, no. 10 (2019): 727. http://dx.doi.org/10.3390/pr7100727.

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The integration of drugs into nanocarriers favorably altered their pharmacodynamics and pharmacokinetics compared to free drugs, and increased their therapeutic index. However, selective cellular internalization in diseased tissues rather than normal tissues still presents a formidable challenge. In this chapter I will cover solutions involving environment-responsive cell-penetrating peptides (CPPs). I will discuss properties of CPPs as universal cellular uptake enhancers, and the modifications imparted to CPP-modified nanocarriers to confine CPP activation to diseased tissues.

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Silva, Sara, António Almeida, and Nuno Vale. "Combination of Cell-Penetrating Peptides with Nanoparticles for Therapeutic Application: A Review." Biomolecules 9, no. 1 (2019): 22. http://dx.doi.org/10.3390/biom9010022.

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Cell-penetrating peptides (CPPs), also known as protein translocation domains, membrane translocating sequences or Trojan peptides, are small molecules of 6 to 30 amino acid residues capable of penetrating biological barriers and cellular membranes. Furthermore, CPP have become an alternative strategy to overcome some of the current drug limitations and combat resistant strains since CPPs are capable of delivering different therapeutic molecules against a wide range of diseases. In this review, we address the recent conjugation of CPPs with nanoparticles, which constitutes a new class of deliv

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Rádis-Baptista, Gandhi. "Cell-Penetrating Peptides Derived from Animal Venoms and Toxins." Toxins 13, no. 2 (2021): 147. http://dx.doi.org/10.3390/toxins13020147.

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Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the ability to selectively interact with the cytoplasmic membrane of certain cell types, translocate across plasma membranes and accumulate in the cell cytoplasm, organelles (e.g., the nucleus and mitochondria) and other subcellular compartments. CPPs are either of natural origin or de novo designed and synthesized from segments and patches of larger proteins or designed by algorithms. With such intrinsic properties, along with membrane permeation, translocation and cellular uptake properties, CPPs can intrace

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Moschos, S. A., A. E. Williams, and M. A. Lindsay. "Cell-penetrating-peptide-mediated siRNA lung delivery." Biochemical Society Transactions 35, no. 4 (2007): 807–10. http://dx.doi.org/10.1042/bst0350807.

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The therapeutic application of siRNA (short interfering RNA) shows promise as an alternative approach to small-molecule inhibitors for the treatment of human disease. However, the major obstacle to its use has been the difficulty in delivering these large anionic molecules in vivo. A potential approach to solving this problem is the chemical conjugation of siRNA to the cationic CPPs (cell-penetrating peptides), Tat-(48–60) (transactivator of transcription) and penetratin, which have been shown previously to mediate protein and peptide delivery in a host of animal models. In this transaction, w

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de Jong, Heleen, Kimberly M. Bonger, and Dennis W. P. M. Löwik. "Activatable cell-penetrating peptides: 15 years of research." RSC Chemical Biology 1, no. 4 (2020): 192–203. http://dx.doi.org/10.1039/d0cb00114g.

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Since the first report on activatable CPPs (ACPPs) in 2004, various methods of activation have been developed. Here, we provide an overview of the different ACPP strategies known to date and summarize the benefits, drawbacks, and future directions.

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Kinyanjui, Margaret W., and Elizabeth D. Fixman. "Cell-penetrating peptides and proteins: new inhibitors of allergic airways diseaseThis review is an invited paper from 2007 ICRH Leadership in Science: a Forum for Trainees and New Investigators." Canadian Journal of Physiology and Pharmacology 86, no. 1-2 (2008): 1–7. http://dx.doi.org/10.1139/y07-125.

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Cell-penetrating peptides (CPPs) or protein transduction domains (PTDs) are peptides that have the ability to efficiently traverse cellular membranes, either alone or in association with molecular cargo. Several naturally occurring PTDs, including those from HIV TAT and Drosophila antennapedia, have this unique activity. Synthetic CPPs, such as polyarginine, also have the ability to enter cells and transport a variety of cargo. While the precise mechanism(s) of cellular entry for individual CPPs may vary, it is likely that uptake is mediated, at least in part, through endocytosis. Moreover, bi

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Gao, Xinli, Song Hong, Zhiping Liu, Tongtao Yue, Jure Dobnikar, and Xianren Zhang. "Membrane potential drives direct translocation of cell-penetrating peptides." Nanoscale 11, no. 4 (2019): 1949–58. http://dx.doi.org/10.1039/c8nr10447f.

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Chen, Chien-Jung, Kang-Chiao Tsai, Ping-Hsueh Kuo, et al. "A Heparan Sulfate-Binding Cell Penetrating Peptide for Tumor Targeting and Migration Inhibition." BioMed Research International 2015 (2015): 1–15. http://dx.doi.org/10.1155/2015/237969.

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As heparan sulfate proteoglycans (HSPGs) are known as co-receptors to interact with numerous growth factors and then modulate downstream biological activities, overexpression of HS/HSPG on cell surface acts as an increasingly reliable prognostic factor in tumor progression. Cell penetrating peptides (CPPs) are short-chain peptides developed as functionalized vectors for delivery approaches of impermeable agents. On cell surface negatively charged HS provides the initial attachment of basic CPPs by electrostatic interaction, leading to multiple cellular effects. Here a functional peptide (CPPec

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Banga, Jaspreet, Dinesh Srinivasan, Chia-Chi Sun, et al. "Inhibition of IRF5 cellular activity with cell-penetrating peptides that target homodimerization." Science Advances 6, no. 20 (2020): eaay1057. http://dx.doi.org/10.1126/sciadv.aay1057.

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The transcription factor interferon regulatory factor 5 (IRF5) plays essential roles in pathogen-induced immunity downstream of Toll-, nucleotide-binding oligomerization domain–, and retinoic acid–inducible gene I–like receptors and is an autoimmune susceptibility gene. Normally, inactive in the cytoplasm, upon stimulation, IRF5 undergoes posttranslational modification(s), homodimerization, and nuclear translocation, where dimers mediate proinflammatory gene transcription. Here, we report the rational design of cell-penetrating peptides (CPPs) that disrupt IRF5 homodimerization. Biochemical an

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Vijakumaran, Ubashini, Fazlina Nordin, Zariyantey Abdul Hamid, Maha Abdullah, and Tye Gee Jun. "Development of Cell Penetrating Peptides for Effective Delivery of Recombinant Factors into Target Cells." Protein & Peptide Letters 27, no. 11 (2020): 1092–101. http://dx.doi.org/10.2174/0929866527666200525164135.

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The cell membrane is a protective layer that strictly controls the passage of molecules restricting the delivery of biomolecules such as drugs, oligonucleotides, peptides, and siRNA into the cells. This shortcoming has been overcome by the discovery of Cell-Penetrating Peptides (CPPs) that has undergone 30 years of evolution. To date, CPPs are largely modified to improve its efficacy and to suit the different delivery applications. The modes of CPPs penetration are still an unresolved mystery and requires further investigations to increase its effectiveness and to diversify its use. Despite ha

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Yang, Jieru, Yacheng Luo, Mohini Anjna Shibu, Istvan Toth, and Mariusz Skwarczynskia. "Cell-penetrating Peptides: Efficient Vectors for Vaccine Delivery." Current Drug Delivery 16, no. 5 (2019): 430–43. http://dx.doi.org/10.2174/1567201816666190123120915.

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Subunit vaccines are composed of pathogen fragments that, on their own, are generally poorly immunogenic. Therefore, the incorporation of an immunostimulating agent, e.g. adjuvant, into vaccine formulation is required. However, there are only a limited number of licenced adjuvants and their immunostimulating ability is often limited, while their toxicity can be substantial. To overcome these problems, a variety of vaccine delivery systems have been proposed. Most of them are designed to improve the stability of antigen in vivo and its delivery into immune cells. Cell-penetrating peptides (CPPs

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Venit, Tomas, Moataz Dowaidar, Maxime Gestin, Syed Raza Mahmood, Ülo Langel, and Piergiorgio Percipalle. "Transcriptional Profiling Reveals Ribosome Biogenesis, Microtubule Dynamics and Expression of Specific lncRNAs to be Part of a Common Response to Cell-Penetrating Peptides." Biomolecules 10, no. 11 (2020): 1567. http://dx.doi.org/10.3390/biom10111567.

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Cell-penetrating peptides (CPPs) are short peptides that are able to efficiently penetrate cellular lipid bilayers. Although CPPs have been used as carriers in conjugation with certain cargos to target specific genes and pathways, how rationally designed CPPs per se affect global gene expression has not been investigated. Therefore, following time course treatments with 4 CPPs-penetratin, PepFect14, mtCPP1 and TP10, HeLa cells were transcriptionally profiled by RNA sequencing. Results from these analyses showed a time-dependent response to different CPPs, with specific sets of genes related to

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Haas, Alexander K., Daniela Maisel, Juliane Adelmann, Christoffer von Schwerin, Ines Kahnt, and Ulrich Brinkmann. "Human-protein-derived peptides for intracellular delivery of biomolecules." Biochemical Journal 442, no. 3 (2012): 583–93. http://dx.doi.org/10.1042/bj20111973.

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Access of therapeutic biomolecules to cytoplasmic and nuclear targets is hampered by the inability of these molecules to cross biological membranes. Approaches to overcome this hurdle involve CPPs (cell-penetrating peptides) or protein transduction domains. Most of these require rather high concentrations to elicit cell-penetrating functionality, are non-human, pathogen-derived or synthetic entities, and may therefore not be tolerated or even immunogenic. We identified novel human-protein-derived CPPs by a combination of in silico and experimental analyses: polycationic CPP candidates were ide

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Habault, Justine, and Jean-Luc Poyet. "Recent Advances in Cell Penetrating Peptide-Based Anticancer Therapies." Molecules 24, no. 5 (2019): 927. http://dx.doi.org/10.3390/molecules24050927.

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Cell-penetrating-peptides (CPPs) are small amino-acid sequences characterized by their ability to cross cellular membranes. They can transport various bioactive cargos inside cells including nucleic acids, large proteins, and other chemical compounds. Since 1988, natural and synthetic CPPs have been developed for applications ranging from fundamental to applied biology (cell imaging, gene editing, therapeutics delivery). In recent years, a great number of studies reported the potential of CPPs as carriers for the treatment of various diseases. Apart from a good efficacy due to a rapid and pote

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Pang, Hong-Bo, Gary B. Braun, and Erkki Ruoslahti. "Neuropilin-1 and heparan sulfate proteoglycans cooperate in cellular uptake of nanoparticles functionalized by cationic cell-penetrating peptides." Science Advances 1, no. 10 (2015): e1500821. http://dx.doi.org/10.1126/sciadv.1500821.

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Cell-penetrating peptides (CPPs) have been widely used to deliver nanomaterials and other types of macromolecules into mammalian cells for therapeutic and diagnostic use. Cationic CPPs that bind to heparan sulfate (HS) proteoglycans on the cell surface induce potent endocytosis; however, the role of other surface receptors in this process is unclear. We describe the convergence of an HS-dependent pathway with the C-end rule (CendR) mechanism that enables peptide ligation with neuropilin-1 (NRP1), a cell surface receptor known to be involved in angiogenesis and vascular permeability. NRP1 binds

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Shah, Vatsal R., Yamini D. Shah, and Mansi N. Athalye. "Novel approaches in development of cell penetrating peptides." Journal of Applied Pharmaceutical Research 9, no. 1 (2021): 1–7. http://dx.doi.org/10.18231/joapr.2021.9.1.08.24.

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Therapeutic cargos which are impermeable to the cell can be delivered by cell penetrating peptides (CPPs). CPP-cargo complexes accumulate by endocytosis inside the cells but they fail to reach the cytosolic space properly as they are often trapped in the endocytic organelles. Here the CPP mediated endosomal escape and some strategies used to increase endosomal escape of CPP-cargo conjugates are discussed with evidence. Potential benefits can be obtained by peptides such as reduction in side effects, biocompatibility, easier synthesis and can be obtained at lower administered doses. The particu

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Su, Ran, Jie Hu, Quan Zou, Balachandran Manavalan, and Leyi Wei. "Empirical comparison and analysis of web-based cell-penetrating peptide prediction tools." Briefings in Bioinformatics 21, no. 2 (2019): 408–20. http://dx.doi.org/10.1093/bib/bby124.

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Abstract Cell-penetrating peptides (CPPs) facilitate the delivery of therapeutically relevant molecules, including DNA, proteins and oligonucleotides, into cells both in vitro and in vivo. This unique ability explores the possibility of CPPs as therapeutic delivery and its potential applications in clinical therapy. Over the last few decades, a number of machine learning (ML)-based prediction tools have been developed, and some of them are freely available as web portals. However, the predictions produced by various tools are difficult to quantify and compare. In particular, there is no system

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Jobin, Marie-Lise, and Isabel D. Alves. "Label-free quantification of cell-penetrating peptide translocation into liposomes." Analytical Methods 8, no. 23 (2016): 4608–16. http://dx.doi.org/10.1039/c6ay00719h.

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Yu, Zhiqiang, Bin Yu, Justin Boy Kaye, et al. "Perspectives and Challenges of Cell-Penetrating Peptides in Effective siRNA Delivery." Nano LIFE 04, no. 04 (2014): 1441016. http://dx.doi.org/10.1142/s1793984414410165.

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Over the last two decades, hundreds of cell penetrating peptides (CPPs) have been intensively developed as drug and nucleic acid delivery vectors. In many cases, however, the efficient delivery of exogenous bioactive molecules through the plasma membrane to their targets remains a tremendous challenging issue. CPPs have attracted tremendous research interest as efficient cellular delivery vehicles due to their intrinsic ability to enter cells and mediate uptake of a wide range of macromolecular cargos, such as proteins, peptides, nucleic acids, drugs and nanoparticle carriers. This review pres

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Fu, Xiangzheng, Lijun Cai, Xiangxiang Zeng, and Quan Zou. "StackCPPred: a stacking and pairwise energy content-based prediction of cell-penetrating peptides and their uptake efficiency." Bioinformatics 36, no. 10 (2020): 3028–34. http://dx.doi.org/10.1093/bioinformatics/btaa131.

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Abstract Motivation Cell-penetrating peptides (CPPs) are a vehicle for transporting into living cells pharmacologically active molecules, such as short interfering RNAs, nanoparticles, plasmid DNAs and small peptides, thus offering great potential as future therapeutics. Existing experimental techniques for identifying CPPs are time-consuming and expensive. Thus, the prediction of CPPs from peptide sequences by using computational methods can be useful to annotate and guide the experimental process quickly. Many machine learning-based methods have recently emerged for identifying CPPs. Althoug

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Gronewold, Anja, Mareike Horn, and Ines Neundorf. "Design and biological characterization of novel cell-penetrating peptides preferentially targeting cell nuclei and subnuclear regions." Beilstein Journal of Organic Chemistry 14 (June 7, 2018): 1378–88. http://dx.doi.org/10.3762/bjoc.14.116.

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Within this study, we report about the design and biological characterization of novel cell-penetrating peptides (CPPs) with selective suborganelle-targeting properties. The nuclear localization sequence N50, as well as the nucleoli-targeting sequence NrTP, respectively, were fused to a shortened version of the cell-penetrating peptide sC18. We examined cellular uptake, subcellular fate and cytotoxicity of these novel peptides, N50-sC18* and NrTP-sC18*, and found that they are nontoxic up to a concentration of 50 or 100 µM depending on the cell lines used. Moreover, detailed cellular uptake st

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Eissa, N. G., E. J. Sayers, D. Birch, et al. "EJP18 peptide derived from the juxtamembrane domain of epidermal growth factor receptor represents a novel membrane-active cell-penetrating peptide." Biochemical Journal 477, no. 1 (2020): 45–60. http://dx.doi.org/10.1042/bcj20190452.

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Membrane-active peptides have been extensively studied to probe protein–membrane interactions, to act as antimicrobial agents and cell-penetrating peptides (CPPs) for the delivery of therapeutic agents to cells. Hundreds of membrane-active sequences acting as CPPs have now been described including bioportides that serve as single entity modifiers of cell physiology at the intracellular level. Translation of promising CPPs in pre-clinical studies have, however, been disappointing as only few identified delivery systems have progressed to clinical trials. To search for novel membrane-active pept

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Varnamkhasti, Behrang Shiri, Samira Jafari, Fereshteh Taghavi, et al. "Cell-Penetrating Peptides: As a Promising Theranostics Strategy to Circumvent the Blood-Brain Barrier for CNS Diseases." Current Drug Delivery 17, no. 5 (2020): 375–86. http://dx.doi.org/10.2174/1567201817666200415111755.

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The passage of therapeutic molecules across the Blood-Brain Barrier (BBB) is a profound challenge for the management of the Central Nervous System (CNS)-related diseases. The ineffectual nature of traditional treatments for CNS disorders led to the abundant endeavor of researchers for the design the effective approaches in order to bypass BBB during recent decades. Cell-Penetrating Peptides (CPPs) were found to be one of the promising strategies to manage CNS disorders. CPPs are short peptide sequences with translocation capacity across the biomembrane. With special regard to their two key adv

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Abes, S., H. Moulton, J. Turner, et al. "Peptide-based delivery of nucleic acids: design, mechanism of uptake and applications to splice-correcting oligonucleotides." Biochemical Society Transactions 35, no. 1 (2007): 53–55. http://dx.doi.org/10.1042/bst0350053.

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CPPs (cell-penetrating peptides) have given rise to much interest for the delivery of biomolecules such as peptides, proteins or ONs (oligonucleotides). CPPs and their conjugates were initially thought to translocate through the cell membrane by a non-endocytotic mechanism which has recently been re-evaluated. Basic-amino-acid-rich CPPs first interact with cell-surface proteoglycans before being internalized by endocytosis. Sequestration and degradation in endocytotic vesicles severely limits the cytoplasmic and nuclear delivery of the conjugated biomolecules. Accordingly, splicing correction

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Wei, Huan-Huan, Wuritu Yang, Hua Tang, and Hao Lin. "The Development of Machine Learning Methods in Cell-Penetrating Peptides Identification: A Brief Review." Current Drug Metabolism 20, no. 3 (2019): 217–23. http://dx.doi.org/10.2174/1389200219666181010114750.

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Background:Cell-penetrating Peptides (CPPs) are important short peptides that facilitate cellular intake or uptake of various molecules. CPPs can transport drug molecules through the plasma membrane and send these molecules to different cellular organelles. Thus, CPP identification and related mechanisms have been extensively explored. In order to reveal the penetration mechanisms of a large number of CPPs, it is necessary to develop convenient and fast methods for CPPs identification.Methods:Biochemical experiments can provide precise details for accurately identifying CPP, but these methods

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Kumar, Sumit, Devender Singh, Pooja Kumari, et al. "PEGylation and Cell-Penetrating Peptides: Glimpse into the Past and Prospects in the Future." Current Topics in Medicinal Chemistry 20, no. 5 (2020): 337–48. http://dx.doi.org/10.2174/1568026620666200128142603.

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Several drug molecules have shown low bioavailability and pharmacokinetic profile due to metabolism by enzymes, excretion by the renal system, or due to other physiochemical properties of drug molecules. These problems have resulted in the loss of efficacy and the gain of side effects associated with drug molecules. PEGylation is one of the strategies to overcome these pharmacokinetic issues and has been successful in the clinic. Cell-penetrating Peptides (CPPs) help to deliver molecules across biological membranes and could be used to deliver cargo selectively to the intracellular site or to

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Nielsen, Peter E. "Addressing the challenges of cellular delivery and bioavailability of peptide nucleic acids (PNA)." Quarterly Reviews of Biophysics 38, no. 4 (2005): 345–50. http://dx.doi.org/10.1017/s0033583506004148.

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1. Introduction 3452. Peptide nucleic acid (PNA) 3463. ‘Cell penetrating peptides’ (CPPs) 3464. Endosomal escape 3475. Cellular delivery of PNA 3476.In vivobioavailability of PNA 3497. References 350Recent results on the cellular delivery of antisense peptide nucleic acids (PNA) via peptide conjugation is briefly discussed, in particular in the context of endosomal entrapment and escape.

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