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Автор: Grafiati
Опубліковано: 6 вересня 2023

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1

Abes, S., H. Moulton, J. Turner, P. Clair, J. P. Richard, P. Iversen, M. J. Gait, and B. Lebleu. "Peptide-based delivery of nucleic acids: design, mechanism of uptake and applications to splice-correcting oligonucleotides." Biochemical Society Transactions 35, no. 1 (January 22, 2007): 53–55. http://dx.doi.org/10.1042/bst0350053.

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Анотація:
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 by CPP-conjugated steric-block ON analogues is inefficient in the absence of endosomolytic agents. New arginine-rich CPPs allowing efficient splicing correction by conjugated PNAs (peptide nucleic acids) or PMO (phosphorodiamidate morpholino oligomer) steric blockers in the absence of endosomolytic agents have recently been defined in our group and are currently being characterized. They offer promising leads for the development of efficient cellular delivery vectors for therapeutic steric-block ON analogues.
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2

Algayer, Bethany, Ann O’Brien, Aaron Momose, Dennis J. Murphy, William Procopio, David M. Tellers, and Thomas J. Tucker. "Novel pH Selective, Highly Lytic Peptides Based on a Chimeric Influenza Hemagglutinin Peptide/Cell Penetrating Peptide Motif." Molecules 24, no. 11 (May 31, 2019): 2079. http://dx.doi.org/10.3390/molecules24112079.

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Delivery of macromolecular cargos such as siRNA to the cytosol after endocytosis remains a critical challenge. Numerous approaches including viruses, lipid nanoparticles, polymeric constructs, and various peptide-based approaches have yet to yield a general solution to this delivery issue. In this manuscript, we describe our efforts to design novel endosomolytic peptides that could be used to facilitate the release of cargos from a late endosomal compartment. These amphiphilic peptides, based on a chimeric influenza hemagglutinin peptide/cell-penetrating peptide (CPP) template, utilize a pH-triggering mechanism in which the peptides are protonated after acidification of the endosome, and thereby adopt an alpha-helical conformation. The helical forms of the peptides are lytically active, while the non-protonated forms are much less or non-lytically active at physiological pH. Starting from an initial lead peptide (INF7-Tat), we systematically modified the sequence of the chimeric peptides to obtain peptides with greatly enhanced lytic activity that maintain good pH selectivity in a red blood cell hemolysis assay.
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3

Akishiba, Misao, Toshihide Takeuchi, Yoshimasa Kawaguchi, Kentarou Sakamoto, Hao-Hsin Yu, Ikuhiko Nakase, Tomoka Takatani-Nakase, Fatemeh Madani, Astrid Gräslund, and Shiroh Futaki. "Cytosolic antibody delivery by lipid-sensitive endosomolytic peptide." Nature Chemistry 9, no. 8 (May 22, 2017): 751–61. http://dx.doi.org/10.1038/nchem.2779.

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4

Abes, R., A. A. Arzumanov, H. M. Moulton, S. Abes, G. D. Ivanova, P. L. Iversen, M. J. Gait, and B. Lebleu. "Cell-penetrating-peptide-based delivery of oligonucleotides: an overview." Biochemical Society Transactions 35, no. 4 (July 20, 2007): 775–79. http://dx.doi.org/10.1042/bst0350775.

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Анотація:
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 (phosphorodiamidate morpholino oligomers), has consequently been inefficient when ONs are conjugated with standard CPPs such as Tat (transactivator of transcription), R9 (nona-arginine), K8 (octalysine) or penetratin in the absence of endosomolytic agents. New arginine-rich CPPs such as (R-Ahx-R)4 (6-aminohexanoic acid-spaced oligo-arginine) or R6 (hexa-arginine)–penetratin conjugated to PMO or PNA resulted in efficient splicing correction at non-cytotoxic doses in the absence of chloroquine. SAR (structure–activity relationship) analyses are underway to optimize these peptide delivery vectors and to understand their mechanisms of cellular internalization.
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5

Ahmad, Aqeel, Kirsi Rilla, Jing Zou, Weikai Zhang, Ilmari Pyykkö, Paavo Kinnunen, and Sanjeev Ranjan. "Enhanced gene expression by a novel designed leucine zipper endosomolytic peptide." International Journal of Pharmaceutics 601 (May 2021): 120556. http://dx.doi.org/10.1016/j.ijpharm.2021.120556.

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6

Ding, Hui, Jose Portilla-Arias, Rameshwar Patil, Keith L. Black, Julia Y. Ljubimova, and Eggehard Holler. "The optimization of polymalic acid peptide copolymers for endosomolytic drug delivery." Biomaterials 32, no. 22 (August 2011): 5269–78. http://dx.doi.org/10.1016/j.biomaterials.2011.03.073.

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7

Han, Muri, Valerie A. Kickhoefer, Glen R. Nemerow, and Leonard H. Rome. "Targeted Vault Nanoparticles Engineered with an Endosomolytic Peptide Deliver Biomolecules to the Cytoplasm." ACS Nano 5, no. 8 (July 26, 2011): 6128–37. http://dx.doi.org/10.1021/nn2014613.

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8

Evans, Brian C., Kyle M. Hocking, Kameron V. Kilchrist, Eric S. Wise, Colleen M. Brophy, and Craig L. Duvall. "Endosomolytic Nano-Polyplex Platform Technology for Cytosolic Peptide Delivery To Inhibit Pathological Vasoconstriction." ACS Nano 9, no. 6 (June 2, 2015): 5893–907. http://dx.doi.org/10.1021/acsnano.5b00491.

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9

Lindberg, Staffan, Andrés Muñoz-Alarcón, Henrik Helmfors, Diogo Mosqueira, Daniel Gyllborg, Oana Tudoran, and Ülo Langel. "PepFect15, a novel endosomolytic cell-penetrating peptide for oligonucleotide delivery via scavenger receptors." International Journal of Pharmaceutics 441, no. 1-2 (January 2013): 242–47. http://dx.doi.org/10.1016/j.ijpharm.2012.11.037.

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10

Duvall, Craig L., Anthony J. Convertine, Danielle S. W. Benoit, Allan S. Hoffman, and Patrick S. Stayton. "Intracellular Delivery of a Proapoptotic Peptide via Conjugation to a RAFT Synthesized Endosomolytic Polymer." Molecular Pharmaceutics 7, no. 2 (February 2010): 468–76. http://dx.doi.org/10.1021/mp9002267.

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11

Kwon, Ester J., Sylvie Liong, and Suzie H. Pun. "A Truncated HGP Peptide Sequence That Retains Endosomolytic Activity and Improves Gene Delivery Efficiencies." Molecular Pharmaceutics 7, no. 4 (June 3, 2010): 1260–65. http://dx.doi.org/10.1021/mp1000668.

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12

Kim, Seong Kyeong, Yu Seok Youn, Kyung Taek Oh, and Eun Seong Lee. "Development of pH-responsive starch–glycol chitosan nanogels for proapoptotic (KLAKLAK)2 peptide delivery." Journal of Bioactive and Compatible Polymers 32, no. 4 (November 28, 2016): 345–54. http://dx.doi.org/10.1177/0883911516676848.

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Анотація:
In this study, we report pH-responsive polysaccharidic nanogels for cytosolic peptide delivery. We conjugated starch to water-soluble glycol chitosan and pH-responsive 3-diethylaminopropylamine (starch–(glycol chitosan–3-diethylaminopropylamine)). Starch–(glycol chitosan–3-diethylaminopropylamine) self-organizes in aqueous solution, with the glycol chitosan blocks on the hydrophilic outer shell and starch and 3-diethylaminopropylamine blocks in the hydrogel inner core. The experimental results demonstrated that the protonation of 3-diethylaminopropylamine at pH 6.0 (endosomal pH) allowed for accelerated release of the encapsulated D-(KLAKLAK)2 proapoptotic peptide from the nanogels as a result of electrostatic repulsion between D-(KLAKLAK)2 and 3-diethylaminopropylamine. A hemolysis test using red blood cell membranes (as an endosomal membrane model) revealed the excellent endosomolytic activity of these nanogels, which likely stems from the proton-sponge effect of 3-diethylaminopropylamine at pH 6.0. As a result, these nanogels resulted in increased KB tumor cell ablation.
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13

Xu, Wen, Mousa Jafari, Feng Yuan, Ran Pan, Baoling Chen, Yong Ding, Tatiana Sheinin, et al. "In vitro and in vivo therapeutic siRNA delivery induced by a tryptophan-rich endosomolytic peptide." Journal of Materials Chemistry B 2, no. 36 (June 30, 2014): 6010. http://dx.doi.org/10.1039/c4tb00629a.

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14

Egorova, Anna A., Polina L. Il'ina, Anton V. Kiselev, Aleksandre N. Baranov, Irina I. Tarasenko, Gennadii P. Vlasov, and Vladislav S. Baranov. "202. Effect of Modification with Lipophilic Fragments and Inclusion of Endosomolytic Peptide on Transfection Efficiency Mediated by Lysine Dendrimers." Molecular Therapy 13 (2006): S78. http://dx.doi.org/10.1016/j.ymthe.2006.08.226.

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15

Lo, Seong Loong, and Shu Wang. "An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection." Biomaterials 29, no. 15 (May 2008): 2408–14. http://dx.doi.org/10.1016/j.biomaterials.2008.01.031.

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16

Abes, Saïd, Hong M. Moulton, Philippe Clair, Paul Prevot, Derek S. Youngblood, Rebecca P. Wu, Patrick L. Iversen, and Bernard Lebleu. "Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents." Journal of Controlled Release 116, no. 3 (December 2006): 304–13. http://dx.doi.org/10.1016/j.jconrel.2006.09.011.

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17

Najjar, Kristina, Alfredo Erazo-Oliveras, Dakota J. Brock, Ting-Yi Wang, and Jean-Philippe Pellois. "An l- to d-Amino Acid Conversion in an Endosomolytic Analog of the Cell-penetrating Peptide TAT Influences Proteolytic Stability, Endocytic Uptake, and Endosomal Escape." Journal of Biological Chemistry 292, no. 3 (December 6, 2016): 847–61. http://dx.doi.org/10.1074/jbc.m116.759837.

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18

Strand, Matthew S., Hua Pan, Julie G. Grossman, Peter S. Goedegebuure, Timothy Fleming, Samuel A. Wickline, and Ryan C. Fields. "Precision cancer therapy through nanoparticle delivery of siRNA against KRAS." Journal of Clinical Oncology 34, no. 4_suppl (February 1, 2016): 260. http://dx.doi.org/10.1200/jco.2016.34.4_suppl.260.

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Анотація:
260 Background: Small interfering RNA (siRNA) has potential for highly specific gene manipulation, making it attractive for delivering precision therapy to cancer patients. However, efforts to employ siRNA therapeutically have been limited by its short half-life in circulation, low target tissue specificity, and cellular entrapment within endosomes. We utilized serum-stable, cell-penetrating, and endosomolytic peptide-based nanoparticles (NPs) to overcome these obstacles and deliver siRNA against KRAS to KRAS-mutant human and mouse pancreas and colorectal cancers. Methods: Human and mouse pancreas and colorectal cancer cell lines were tested for NP uptake in vitro utilizing fluorescent siRNAs. Uptake was assessed via fluorescent microscopy and flow cytometry (FC). Mice bearing tumors from these cells were injected IV with the same NP, and uptake was assessed with an in vivo imaging system (IVIS), and FC. Cell lines were treated with KRAS-siRNA NP and KRAS knockdown was assessed by real-time PCR. Results: Mouse and human pancreas and colorectal cancer cell lines took up NP in vitro, with signal detected within > 93% of cells at 24 hours. Tumors from these cells grown in mice were strongly fluorescent after IV injection of fluorescent NP within 2 hours, and until at least 30 hours. FC of a tumor treated with fluorescent NP showed that 86% of tumor cells expressed fluorescent signal 24 hours post-injection. IVIS revealed signal in mouse liver and kidneys, but when assessed by FC, only 17.8% and 13.5% of cells from these tissues were fluorescent, respectively. The brain, heart, lungs, spleen, and pancreas of mice receiving injections were negative. Cancer cell lines exposed to KRAS-siRNA NP for 48 hours express KRAS at levels that are 4.5 to 15.1% of untreated cells. Conclusions: Human and mouse pancreas and colorectal cancers efficiently and specifically take up NP in vitro and in vivo. Selected limitations of siRNA are overcome with this NP delivery system, and NP-packaged siRNA effectively inhibits KRAS. This platform represents a highly specific approach to targeting tumor genes of interest, which may ultimately enable selective knockdown of putative drivers of tumor progression.
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19

Ahmad, Aqeel, Sanjeev Ranjan, Weikai Zhang, Jing Zou, Ilmari Pyykkö, and Paavo K. J. Kinnunen. "Novel endosomolytic peptides for enhancing gene delivery in nanoparticles." Biochimica et Biophysica Acta (BBA) - Biomembranes 1848, no. 2 (February 2015): 544–53. http://dx.doi.org/10.1016/j.bbamem.2014.11.008.

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20

Lundberg, Pontus, S. El‐Andaloussi, T. Sütlü, H. Johansson, and Ü. Langel. "Delivery of short interfering RNA using endosomolytic cell‐penetrating peptides." FASEB Journal 21, no. 11 (April 26, 2007): 2664–71. http://dx.doi.org/10.1096/fj.06-6502com.

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21

Xu, Wen, Ran Pan, Danyang Zhao, Dafeng Chu, Yan Wu, Rong Wang, Baoling Chen, et al. "Design and Evaluation of Endosomolytic Biocompatible Peptides as Carriers for siRNA Delivery." Molecular Pharmaceutics 12, no. 1 (November 20, 2014): 56–65. http://dx.doi.org/10.1021/mp500429u.

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22

Chen, Xiaolong, Hanjie Liu, Ang Li, Shuangshuang Ji, and Hao Fei. "Hydrophobicity-tuned anion responsiveness underlies endosomolytic cargo delivery mediated by amphipathic vehicle peptides." Journal of Biological Chemistry 297, no. 6 (December 2021): 101364. http://dx.doi.org/10.1016/j.jbc.2021.101364.

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23

Ho, Vincent H. B., Nigel K. H. Slater, and Rongjun Chen. "pH-responsive endosomolytic pseudo-peptides for drug delivery to multicellular spheroids tumour models." Biomaterials 32, no. 11 (April 2011): 2953–58. http://dx.doi.org/10.1016/j.biomaterials.2011.01.010.

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24

Lee, Ya-Jung, Gregory Johnson, and Jean-Philippe Pellois. "Modeling of the Endosomolytic Activity of HA2-TAT Peptides with Red Blood Cells and Ghosts." Biochemistry 49, no. 36 (September 14, 2010): 7854–66. http://dx.doi.org/10.1021/bi1008408.

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25

Wang, Shiqi, and Rongjun Chen. "pH-Responsive, Lysine-Based, Hyperbranched Polymers Mimicking Endosomolytic Cell-Penetrating Peptides for Efficient Intracellular Delivery." Chemistry of Materials 29, no. 14 (May 16, 2017): 5806–15. http://dx.doi.org/10.1021/acs.chemmater.7b00054.

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26

Meyer, Martin, Alexander Philipp, Reza Oskuee, Claudia Schmidt, and Ernst Wagner. "Breathing Life into Polycations: Functionalization with pH-Responsive Endosomolytic Peptides and Polyethylene Glycol Enables siRNA Delivery." Journal of the American Chemical Society 130, no. 11 (March 2008): 3272–73. http://dx.doi.org/10.1021/ja710344v.

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27

Liou, Ji-Sing, Betty Revon Liu, Adam L. Martin, Yue-Wern Huang, Huey-Jenn Chiang, and Han-Jung Lee. "Protein transduction in human cells is enhanced by cell-penetrating peptides fused with an endosomolytic HA2 sequence." Peptides 37, no. 2 (October 2012): 273–84. http://dx.doi.org/10.1016/j.peptides.2012.07.019.

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28

Angeles-Boza, Alfredo M., Alfredo Erazo-Oliveras, Ya-Jung Lee, and Jean-Philippe Pellois. "Generation of Endosomolytic Reagents by Branching of Cell-Penetrating Peptides: Tools for the Delivery of Bioactive Compounds to Live Cells in Cis or Trans." Bioconjugate Chemistry 21, no. 12 (December 15, 2010): 2164–67. http://dx.doi.org/10.1021/bc100130r.

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29

Lieser, Rachel M., Qirun Li, Wilfred Chen, and Millicent O. Sullivan. "Incorporation of Endosomolytic Peptides with Varying Disruption Mechanisms into EGFR-Targeted Protein Conjugates: The Effect on Intracellular Protein Delivery and EGFR Specificity in Breast Cancer Cells." Molecular Pharmaceutics 19, no. 2 (January 18, 2022): 661–73. http://dx.doi.org/10.1021/acs.molpharmaceut.1c00788.

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30

Montespan, Charlotte, Christopher M. Wiethoff, and Harald Wodrich. "A Small Viral PPxY Peptide Motif To Control Antiviral Autophagy." Journal of Virology 91, no. 18 (June 28, 2017). http://dx.doi.org/10.1128/jvi.00581-17.

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ABSTRACT Autophagy is an essential metabolic program that is also used for clearing intracellular pathogens. This mechanism, also termed selective autophagy, is well characterized for invasive bacteria but remains poorly documented for viral infections. Here we highlight our recent work showing that endosomolytic adenoviruses trigger autophagy when entering cells. Our study revealed how adenoviruses exploit a capsid-associated small PPxY peptide motif to manipulate the autophagic machinery to prevent autophagic degradation and to promote endosomal escape and nuclear trafficking.
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31

Ubiparipovic, Stephanie, Daniel Christ, and Romain Rouet. "Antibody-mediated delivery of CRISPR-Cas9 ribonucleoproteins in human cells." Protein Engineering, Design and Selection, November 7, 2022. http://dx.doi.org/10.1093/protein/gzac011.

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Abstract The CRISPR genome editing technology holds great clinical potential for the treatment of monogenetic disorders such as sickle cell disease or muscular dystrophy. The therapeutic in vivo application of the technology relies on targeted delivery methods of the Cas9 and gRNA complex to specific cells and/or tissues. However, such methods are currently limited to direct organ delivery, preventing wide clinical application. Here, we show that monoclonal antibodies can be employed to deliver the Cas9/gRNA complex directly into human cells via cell-surface receptors. Using the SpyCatcher/SpyTag system, we conjugated the Fab fragment of the therapeutic antibodies Trastuzumab and Pertuzumab directly to the Cas9 enzyme and observed HER2-specific uptake of the ribonucleoprotein in a human HER2 expressing cell line. Following cellular uptake in the presence of an endosomolytic peptide, modest gene editing was also observed. This finding provides a blueprint for the targeted delivery of the CRISPR technology into specific cells using monoclonal antibodies.
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32

Kirman, Dogan Can, Bhuvanasundar Renganathan, Wai Kit Chui, Ming Wei Chen, Neslihan Arife Kaya, and Ruowen Ge. "Cell surface nucleolin is a novel ADAMTS5 receptor mediating endothelial cell apoptosis." Cell Death & Disease 13, no. 2 (February 2022). http://dx.doi.org/10.1038/s41419-022-04618-x.

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AbstractA Disintegrin and Metalloproteinase with ThromboSpondin motif (ADAMTS) 5 functions as an anti-angiogenic and anti-cancer protein independent of its metalloproteinase activity. Both full-length ADAMTS5 and TS5-p45, the autocatalytically cleaved C-terminal 45 kDa truncate of ADAMTS5, inhibits angiogenesis, and induces endothelial cell (EC) apoptosis. However, how ADAMTS5 triggers EC apoptosis remains unclear. This work shows that caspase-8 (Cas-8) and caspase-9 (Cas-9) are involved in TS5-p45-induced EC apoptosis. We identify cell surface nucleolin (NCL) as a novel high-affinity receptor for TS5-p45 in ECs, mediating TS5-p45’s cell surface binding and pro-apoptotic function. We show that the central RNA-binding domain (RBD) of NCL is essential and sufficient for its binding to TS5-p45. Upon interacting with EC surface NCL, TS5-p45 is internalized through clathrin- and caveolin-dependent endocytosis and trafficked to the nucleus via late endosomes (LEs). We demonstrate that the nuclear trafficking of TS5-p45 is important for its pro-apoptotic activity as disruption of LE membrane integrity with an endosomolytic peptide suppressed both nuclear trafficking and pro-apoptotic activity of TS5-p45. Through cell surface biotinylation, we revealed that cell surface NCL shuttles extracellular TS5-p45 to the nucleus to mediate apoptosis. Furthermore, blocking the importin α1/ß1 receptor hindered the nuclear trafficking of TS5-p45, suggesting the involvement of the nuclear importing machinery for this nuclear translocation. RNA-seq identified many apoptosis-related genes that are differentially expressed at least two-fold in TS5-p45-treated ECs, with 10 of them qRT-PCR-validated and at least 5 of these genes potentially contributing to TS5-p45-NCL-induced apoptosis. Altogether, our work identifies NCL as a novel cell surface receptor for ADAMTS5 and demonstrates the critical role of NCL-mediated internalization and nuclear trafficking for ADAMTS5-induced EC apoptosis. These findings reveal novel mechanistic insights of the secreted metalloproteinase ADAMTS5 in angiogenesis inhibition.
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33

Ahmad, Aqeel, and Javed Masood Khan. "pH-sensitive endosomolytic peptides in gene and drug delivery: Endosomal escape and current challenges." Journal of Drug Delivery Science and Technology, September 2022, 103786. http://dx.doi.org/10.1016/j.jddst.2022.103786.

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34

Mehdipour, Golnaz, Milint Neleptchenko Wintrasiri, and Sorayya Ghasemi. "CPP-Based Bioactive Drug Delivery to Penetrate the Blood-Brain Barrier: A Potential Therapy for Glioblastoma Multiforme." Current Drug Targets 23 (February 7, 2022). http://dx.doi.org/10.2174/1389450123666220207143750.

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Анотація:
Background: A large number of studies have been conducted on the treatment of glioblastoma multiforme (GBM). Chemotherapeutic drugs cannot penetrate deeply into the brain parenchyma due to the presence of the blood-brain barrier (BBB). Hence, crossing BBB is the significant obstacle in developing new therapeutic methods for GBM. Objective: Cell penetrating peptides (CPPs) have emerged as new tools that can efficiently deliver various substances across BBB. CPPs beneficial properties, such as BBB penetration capacity, low toxicity, and the ability to achieve active targeting and controllable drug release, have made them worthy candidates for GBM treatment. However, their application is limited by several drawbacks, including lack of selectivity, insufficient transport efficacy, and low stability. In order to overcome the selectivity issue, tumor targeting peptides and sequences that can be activated at the target site have been embedded into the structure of CPPs. To overcome their insufficient transport efficacy into the cells, which is mostly due to endosomal entrapment, various endosomolytic moieties have been incorporated into CPPs. Finally, their instability in blood circulation can be solved through different modifications to their structures. As this field is moving beyond preclinical studies, the discovery of new and more efficient CPPs for GBM treatment has become crucial. Thus, by using display techniques, such as phage display, this encouraging treatment strategy can be developed further. Conclusion: Consequently, despite several challenges in CPPs application, recent progress in studies has shown their potential for the development of the next generation GBM therapeutics.
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35

Najjar, Kristina, Alfredo Erazo-Oliveras, and Jean-Philippe Pellois. "Delivery of Proteins, Peptides or Cell-impermeable Small Molecules into Live Cells by Incubation with the Endosomolytic Reagent dfTAT." Journal of Visualized Experiments, no. 103 (September 2, 2015). http://dx.doi.org/10.3791/53175.

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