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Journal articles on the topic 'Endosomal escape peptide'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Nielsen, Peter E. "Addressing the challenges of cellular delivery and bioavailability of peptide nucleic acids (PNA)." Quarterly Reviews of Biophysics 38, no. 4 (November 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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2

Bartz, René, Haihong Fan, Jingtao Zhang, Nathalie Innocent, Craig Cherrin, Stephen C. Beck, Yi Pei, et al. "Effective siRNA delivery and target mRNA degradation using an amphipathic peptide to facilitate pH-dependent endosomal escape." Biochemical Journal 435, no. 2 (March 29, 2011): 475–87. http://dx.doi.org/10.1042/bj20101021.

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Effective delivery of siRNA (small interfering RNA) into the cells requires the translocation of siRNA into the cytosol. One potential delivery strategy uses cell-delivery peptides that facilitate this step. In the present paper, we describe the characterization of an amphipathic peptide that mediates the uptake of non-covalently bound siRNA into cells and its subsequent release into the cytosol. Biophysical characterization of peptide and peptide/siRNA mixtures at neutral and lysosomal (acidic) pH suggested the formation of α-helical structure only in endosomes and lysosomes. Surprisingly, even though the peptide enhanced the uptake of siRNA into cells, no direct interaction between siRNA and peptide was observed at neutral pH by isothermal titration calorimetry. Importantly, we show that peptide-mediated siRNA uptake occurred through endocytosis and, by applying novel endosomal-escape assays and cell-fractionation techniques, we demonstrated a pH-dependent alteration in endosome and lysosome integrity and subsequent release of siRNA and other cargo into the cytosol. These results indicate a peptide-mediated siRNA delivery through a pH-dependent and conformation-specific interaction with cellular membranes and not with the cargo.

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3

Soe, Tet Htut, Kazunori Watanabe, and Takashi Ohtsuki. "Photoinduced Endosomal Escape Mechanism: A View from Photochemical Internalization Mediated by CPP-Photosensitizer Conjugates." Molecules 26, no. 1 (December 23, 2020): 36. http://dx.doi.org/10.3390/molecules26010036.

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Endosomal escape in cell-penetrating peptide (CPP)-based drug/macromolecule delivery systems is frequently insufficient. The CPP-fused molecules tend to remain trapped inside endosomes and end up being degraded rather than delivered into the cytosol. One of the methods for endosomal escape of CPP-fused molecules is photochemical internalization (PCI), which is based on the use of light and a photosensitizer and relies on photoinduced endosomal membrane destabilization to release the cargo molecule. Currently, it remains unclear how this delivery strategy behaves after photostimulation. Recent findings, including our studies using CPP-cargo-photosensitizer conjugates, have shed light on the photoinduced endosomal escape mechanism. In this review, we discuss the structural design of CPP-photosensitizer and CPP-cargo-photosensitizer conjugates, and the PCI mechanism underlying their application.

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4

Torres, Julián D., Juan C. Cruz, and Luis H. Reyes. "Synthesis, Characterization, and Functionalization of Graphene Oxide-Based Nanoplatforms for Gene Delivery." Materials Proceedings 4, no. 1 (November 11, 2020): 23. http://dx.doi.org/10.3390/iocn2020-07925.

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Gene therapy has been considered a promising strategy for treating several inherited diseases and acquired complex disorders. One crucial challenge yet to be solved to ensure the nanomaterials’ success in delivering gene therapies is their ability to escape from endosomes. To address this issue, we previously developed magnetite nanoparticles conjugated with the antimicrobial peptide Buforin II, which showed potent translocating and endosomal escape abilities in several cell lines. In this work, we propose developing new cell-penetrating nanoplatforms by interfacing graphene oxide (GO) with powerful translocating peptides to take advantage of already tested and unique peptides as well as the distinctive interactions of GO with the phospholipids of membranes and endosomes. GO was prepared by the modified Hummers’ method through the oxidation of graphite sheets. Next, the functionalization of GO was carried out by rendering pendant amine groups to the GO surface. Thermogravimetric analysis (TGA) and Fourier-transform infrared spectroscopy (FTIR) were used to corroborate the successful functionalization of the nanoplatform. FTIR analysis exhibited the peaks related to the distinct carboxyl groups of GO and the Si–O bonds after silanization. TGA allowed us to estimate a silanization efficiency of 38%. Future work will be focused on conjugating Buforin II and assessing translocation efficiency by conducting uptake assays in liposomes and various cell lines. Additionally, endosomal escape will be determined via confocal microscopy by labeling the peptide with fluorescent molecules and examining colocalization with the fluorescent marker of endosomes, LysoTracker. By taking advantage of the exceptional qualities in terms of the physicochemical, electrical, and optical properties of GO, this study might provide novel strategies to overcome limitations commonly faced, such as low stability of the translocating biomolecules and endosomal entrapment.

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5

Radford, Robert J., Wen Chyan, and Stephen J. Lippard. "Peptide targeting of fluorescein-based sensors to discrete intracellular locales." Chem. Sci. 5, no. 11 (2014): 4512–16. http://dx.doi.org/10.1039/c4sc01280a.

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Fluorescein-labeled peptides are often sequestered within acidic vesicles, diminishing their applicability for live cell imaging. Installing reactive acetyl groups onto the sensing moiety of a labeled peptide facilitates endosomal escape and allows for peptide-based targeting of fluorescent sensors to discrete intracellular locales.

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6

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 (March 15, 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 particular peptide known as cell penetrating peptides are able to translocate themselves across membrane with the carrier drugs with different mechanisms. This is of prime importance in drug delivery systems as they have capability to cross physiological membranes. This review describes various mechanisms for effective drug delivery and associated challenges

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7

Zhang, Qiaoping, Bin Gao, Khan Muhammad, Xubin Zhang, Xiang-kui Ren, Jintang Guo, Shihai Xia, Wencheng Zhang, and Yakai Feng. "Multifunctional gene delivery systems with targeting ligand CAGW and charge reversal function for enhanced angiogenesis." Journal of Materials Chemistry B 7, no. 11 (2019): 1906–19. http://dx.doi.org/10.1039/c8tb03085e.

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8

Rong, Guangyu, Changping Wang, Lijie Chen, Yang Yan, and Yiyun Cheng. "Fluoroalkylation promotes cytosolic peptide delivery." Science Advances 6, no. 33 (August 2020): eaaz1774. http://dx.doi.org/10.1126/sciadv.aaz1774.

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Cytosolic delivery of peptides remains a challenging task owing to their susceptibility to enzymatic degradation and the existence of multiple intracellular barriers. Here, we report a new strategy to address these issues by decoration of a fluorous tag on the terminal of cargo peptides. The fluorous-tagged peptides were assembled into nanostructures, efficiently internalized by cells via several endocytic pathways and released into the cytosol after endosomal escape. They were relatively stable against enzymatic degradation and showed much higher efficiency than nonfluorinated analogs and cell penetrant peptide–conjugated ones. The proposed strategy also efficiently delivered a proapoptotic peptide into specific sites in the cells and restored the function of cargo peptide after cytosolic delivery. The fluorous-tagged proapoptotic peptide efficiently inhibited tumor growth in vivo. This study provides an efficient fluorination strategy to promote the cytosolic delivery of peptides.

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9

Mejia, Franklin, Sabrina Khan, David T. Omstead, Christina Minetos, and Basar Bilgicer. "Identification and optimization of tunable endosomal escape parameters for enhanced efficacy in peptide-targeted prodrug-loaded nanoparticles." Nanoscale 14, no. 4 (2022): 1226–40. http://dx.doi.org/10.1039/d1nr05357d.

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10

Cerda, María Belén, Milena Batalla, Martina Anton, Eduardo Cafferata, Osvaldo Podhajcer, Christian Plank, Olga Mykhaylyk, and Lucia Policastro. "Enhancement of nucleic acid delivery to hard-to-transfect human colorectal cancer cells by magnetofection at laminin coated substrates and promotion of the endosomal/lysosomal escape." RSC Advances 5, no. 72 (2015): 58345–54. http://dx.doi.org/10.1039/c5ra06562c.

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Optimization of nucleic acid delivery in hard-to-transfect colorectal cancer cells by magnetofection at coated laminin substrates and by the endosomal escape enhancement of magnetic complexes using INF-7 peptide.

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11

He, Hongjian, Jiaqi Guo, Jiashu Xu, Jiaqing Wang, Shuang Liu, and Bing Xu. "Dynamic Continuum of Nanoscale Peptide Assemblies Facilitates Endocytosis and Endosomal Escape." Nano Letters 21, no. 9 (May 3, 2021): 4078–85. http://dx.doi.org/10.1021/acs.nanolett.1c01029.

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12

Kämper, Nadine, Patricia M. Day, Thorsten Nowak, Hans-Christoph Selinka, Luise Florin, Jan Bolscher, Lydia Hilbig, John T. Schiller, and Martin Sapp. "A Membrane-Destabilizing Peptide in Capsid Protein L2 Is Required for Egress of Papillomavirus Genomes from Endosomes." Journal of Virology 80, no. 2 (January 15, 2006): 759–68. http://dx.doi.org/10.1128/jvi.80.2.759-768.2006.

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ABSTRACT Papillomaviruses are internalized via clathrin-dependent endocytosis. However, the mechanism by which viral genomes pass endosomal membranes has not been elucidated. In this report we show that the minor capsid protein L2 is required for egress of viral genomes from endosomes but not for initial uptake and uncoating and that a 23-amino-acid peptide at the C terminus of L2 is necessary for this function. Pseudogenomes encapsidated by L1 and L2 lacking this peptide accumulated in vesicular compartments similar to that observed with L1-only viral particles, and these mutant pseudoviruses were noninfectious. This L2 peptide displayed strong membrane-disrupting activity, induced cytolysis of bacteria and eukaryotic cells in a pH-dependent manner, and permeabilized cells after exogenous addition. Fusions between green fluorescent protein and the L2 peptide integrated into cellular membranes like the wild type but not like C-terminal mutants of L2. Our data indicate that the L2 C terminus facilitates escape of viral genomes from the endocytic compartment and that this feature is conserved among papillomaviruses. Furthermore, the characteristic of this peptide differs from the classical virus-encoded membrane-penetrating peptides.

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13

Gentry, Schuyler B., Scott J. Nowak, Xuelei Ni, Stephanie A. Hill, Lydia R. Wade, William R. Clark, Aidan P. Keelaghan, Daniel P. Morris, and Jonathan L. McMurry. "A real-time assay for cell-penetrating peptide-mediated delivery of molecular cargos." PLOS ONE 16, no. 9 (September 2, 2021): e0254468. http://dx.doi.org/10.1371/journal.pone.0254468.

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Cell-penetrating peptides (CPPs) are capable of transporting molecules to which they are tethered across cellular membranes. Unsurprisingly, CPPs have attracted attention for their potential drug delivery applications, but several technical hurdles remain to be overcome. Chief among them is the so-called ‘endosomal escape problem,’ i.e. the propensity of CPP-cargo molecules to be endocytosed but remain entrapped in endosomes rather than reaching the cytosol. Previously, a CPP fused to calmodulin that bound calmodulin binding site-containing cargos was shown to efficiently deliver cargos to the cytoplasm, effectively overcoming the endosomal escape problem. The CPP-adaptor, “TAT-CaM,” evinces delivery at nM concentrations and more rapidly than we had previously been able to measure. To better understand the kinetics and mechanism of CPP-adaptor-mediated cargo delivery, a real-time cell penetrating assay was developed in which a flow chamber containing cultured cells was installed on the stage of a confocal microscope to allow for observation ab initio. Also examined in this study was an improved CPP-adaptor that utilizes naked mole rat (Heterocephalus glaber) calmodulin in place of human and results in superior internalization, likely due to its lesser net negative charge. Adaptor-cargo complexes were delivered into the flow chamber and fluorescence intensity in the midpoint of baby hamster kidney cells was measured as a function of time. Delivery of 400 nM cargo was observed within seven minutes and fluorescence continued to increase linearly as a function of time. Cargo-only control experiments showed that the minimal uptake which occurred independently of the CPP-adaptor resulted in punctate localization consistent with endosomal entrapment. A distance analysis was performed for cell-penetration experiments in which CPP-adaptor-delivered cargo showing wider dispersions throughout cells as compared to an analogous covalently-bound CPP-cargo. Small molecule endocytosis inhibitors did not have significant effects upon delivery. The real-time assay is an improvement upon static endpoint assays and should be informative in a broad array of applications.

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14

Lee, Woojong, Brock Bakke, Shelly Sonsalla, Darren Sanchez, Leticia Reyes, Gopal Iyer, and M. Suresh. "Carbomer-based adjuvant potentiates CTL immunity by enhancing cross-presentation of antigens by NOX2 and TAP-dependent mechanisms." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 70.5. http://dx.doi.org/10.4049/jimmunol.202.supp.70.5.

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Abstract We have previously showed that a carbomer-based adjuvant (CBA), Adjuplex® (ADJ) enhanced systemic and mucosal CD8 T cell responses to non-replicating antigens. Here, we investigated the molecular mechanism(s) of how the CBA enhance cross-presentation of antigens by dendritic cells (DCs). We found that ADJ enhanced cross-presentation of antigens in DCs by several mechanisms, including augmenting antigen degradation, reducing endosomal acidity, promoting antigen localization to early endosomes and increasing ROS production leading to escape of antigen from endosomes to the cytosol. Additionally, we find that ADJ-induced cross-presentation of antigens by DCs required NOX2 and TAP1. Taken together, we propose that ADJ enhances cross-presentation of antigens by promoting NOX2-dependent ROS production leading to endosomal antigen leakage, proteolysis of antigen by proteasomes and TAP-dependent peptide transport into MHC-containing cellular compartment. Thus, our studies have revealed a novel mechanism for ADJ-induced cross-presentation of antigen, highlighting the significance of incorporating CBA as a vaccine adjuvant to elicit strong cytotoxic T cell responses.

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15

Li, Chen, Xue-Wei Cao, Jian Zhao, and Fu-Jun Wang. "Effective Therapeutic Drug Delivery by GALA3, an Endosomal Escape Peptide with Reduced Hydrophobicity." Journal of Membrane Biology 253, no. 2 (January 31, 2020): 139–52. http://dx.doi.org/10.1007/s00232-020-00109-2.

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16

Voltà-Durán, Eric, Julieta M. Sánchez, Eloi Parladé, Naroa Serna, Esther Vazquez, Ugutz Unzueta, and Antonio Villaverde. "The Diphtheria Toxin Translocation Domain Impairs Receptor Selectivity in Cancer Cell-Targeted Protein Nanoparticles." Pharmaceutics 14, no. 12 (November 29, 2022): 2644. http://dx.doi.org/10.3390/pharmaceutics14122644.

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Protein-based materials intended as nanostructured drugs or drug carriers are progressively gaining interest in nanomedicine, since their structure, assembly and cellular interactivity can be tailored by recruiting functional domains. The main bottleneck in the development of deliverable protein materials is the lysosomal degradation that follows endosome maturation. This is especially disappointing in the case of receptor-targeted protein constructs, which, while being highly promising and in demand in precision medicines, enter cells via endosomal/lysosomal routes. In the search for suitable protein agents that might promote endosome escape, we have explored the translocation domain (TD) of the diphtheria toxin as a functional domain in CXCR4-targeted oligomeric nanoparticles designed for cancer therapies. The pharmacological interest of such protein materials could be largely enhanced by improving their proteolytic stability. The incorporation of TD into the building blocks enhances the amount of the material detected inside of exposed CXCR4+ cells up to around 25-fold, in absence of cytotoxicity. This rise cannot be accounted for by endosomal escape, since the lysosomal degradation of the new construct decreases only moderately. On the other hand, a significant loss in the specificity of the CXCR4-dependent cellular penetration indicates the unexpected role of the toxin segment as a cell-penetrating peptide in a dose-dependent and receptor-independent fashion. These data reveal that the diphtheria toxin TD displayed on receptor-targeted oligomeric nanoparticles partially abolishes the exquisite receptor specificity of the parental material and it induces nonspecific internalization in mammalian cells.

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17

Ghavami, Shiraishi, and Nielsen. "Cooperative Cellular Uptake and Activity of Octaarginine Antisense Peptide Nucleic acid (PNA) Conjugates." Biomolecules 9, no. 10 (October 1, 2019): 554. http://dx.doi.org/10.3390/biom9100554.

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Cellular uptake and antisense activity of d-octaarginine conjugated peptide nucleic acids (PNAs) is shown to exhibit pronounced cooperativity in serum-containing medium, in particular by being enhanced by analogous mis-match PNA–cell-penetrating peptide (PNA–CPP) conjugates without inherent antisense activity. This cooperativity does not show cell or PNA sequence dependency, suggesting that it is a common effect in cationic CPP conjugated PNA delivery. Interestingly, our results also indicate that Deca-r8-PNA and r8-PNA could assist each other and even other non-CPP PNAs as an uptake enhancer agent. However, the peptide itself (without being attached to the PNA) failed to enhance uptake and antisense activity. These results are compatible with an endosomal uptake mechanism in which the endocytosis event is induced by multiple CPP–PNA binding to the cell surface requiring a certain CPP density, possibly in terms of nanoparticle number and/or size, to be triggered. In particular the finding that the number of endosomal events is dependent on the total CPP–PNA concentration supports such a model. It is not possible from the present results to conclude whether endosomal escape is also cooperatively induced by CPP–PNA.

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18

Ryu, Kitae, Gyeong Jin Lee, Ji-yeong Choi, Taewan Kim, and Tae-il Kim. "Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems." Advances in Materials Science and Engineering 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/852584.

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Self-assembling multifunctional peptide was designed for gene delivery systems. The multifunctional peptide (MP) consists of cellular penetrating peptide moiety (R8), matrix metalloproteinase-2 (MMP-2) specific sequence (GPLGV), pH-responsive moiety (H5), and hydrophobic moiety (palmitic acid) (CR8GPLGVH5-Pal). MP was oxidized to form multifunctional peptide dimer (MPD) by DMSO oxidation of thiols in terminal cysteine residues. MPD could condense pDNA successfully at a weight ratio of 5. MPD itself could self-assemble into submicron micelle particles via hydrophobic interaction, of which critical micelle concentration is about 0.01 mM. MPD showed concentration-dependent but low cytotoxicity in comparison with PEI25k. MPD polyplexes showed low transfection efficiency in HEK293 cells expressing low level of MMP-2 but high transfection efficiency in A549 and C2C12 cells expressing high level of MMP-2, meaning the enhanced transfection efficiency probably due to MMP-induced structural change of polyplexes. Bafilomycin A1-treated transfection results suggest that the transfection of MPD is mediated via endosomal escape by endosome buffering ability. These results show the potential of MPD for MMP-2 targeted gene delivery systems due to its multifunctionality.

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19

Meng, Zhao, Liang Luan, Ziyao Kang, Siliang Feng, Qingbin Meng, and Keliang Liu. "Histidine-enriched multifunctional peptide vectors with enhanced cellular uptake and endosomal escape for gene delivery." Journal of Materials Chemistry B 5, no. 1 (2017): 74–84. http://dx.doi.org/10.1039/c6tb02862d.

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20

Salerno, John C., Verra M. Ngwa, Scott J. Nowak, Carol A. Chrestensen, Allison N. Healey, and Jonathan L. McMurry. "Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos." Journal of Cell Science 129, no. 5 (January 22, 2016): 893–97. http://dx.doi.org/10.1242/jcs.182113.

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21

Salerno, John C., Verra M. Ngwa, Scott J. Nowak, Carol A. Chrestensen, Allison N. Healey, and Jonathan L. McMurry. "Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos." Journal of Cell Science 129, no. 12 (June 15, 2016): 2473–74. http://dx.doi.org/10.1242/jcs.192666.

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22

Qian, Ziqing, Jonathan R. LaRochelle, Bisheng Jiang, Wenlong Lian, Ryan L. Hard, Nicholas G. Selner, Rinrada Luechapanichkul, Amy M. Barrios, and Dehua Pei. "Early Endosomal Escape of a Cyclic Cell-Penetrating Peptide Allows Effective Cytosolic Cargo Delivery." Biochemistry 53, no. 24 (June 11, 2014): 4034–46. http://dx.doi.org/10.1021/bi5004102.

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23

Salomone, Fabrizio, Francesco Cardarelli, Mariagrazia Di Luca, Claudia Boccardi, Riccardo Nifosì, Giuseppe Bardi, Lorenzo Di Bari, Michela Serresi, and Fabio Beltram. "A novel chimeric cell-penetrating peptide with membrane-disruptive properties for efficient endosomal escape." Journal of Controlled Release 163, no. 3 (November 2012): 293–303. http://dx.doi.org/10.1016/j.jconrel.2012.09.019.

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24

Azuma, Yusuke, Haruka Imai, Yoshimasa Kawaguchi, Ikuhiko Nakase, Hiroshi Kimura, and Shiroh Futaki. "Modular Redesign of a Cationic Lytic Peptide To Promote the Endosomal Escape of Biomacromolecules." Angewandte Chemie 130, no. 39 (August 30, 2018): 12953–56. http://dx.doi.org/10.1002/ange.201807534.

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Sakurai, Yu, Hiroto Hatakeyama, Yusuke Sato, Hidetaka Akita, Kentaro Takayama, Sachiko Kobayashi, Shiroh Futaki, and Hideyoshi Harashima. "Endosomal escape and the knockdown efficiency of liposomal-siRNA by the fusogenic peptide shGALA." Biomaterials 32, no. 24 (August 2011): 5733–42. http://dx.doi.org/10.1016/j.biomaterials.2011.04.047.

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26

Tan, Xiaohong, Marcel P. Bruchez, and Bruce A. Armitage. "Efficient Cytoplasmic Delivery of Antisense Probes Assisted by Cyclized-Peptide-Mediated Photoinduced Endosomal Escape." ChemBioChem 20, no. 5 (January 23, 2019): 727–33. http://dx.doi.org/10.1002/cbic.201800709.

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Azuma, Yusuke, Haruka Imai, Yoshimasa Kawaguchi, Ikuhiko Nakase, Hiroshi Kimura, and Shiroh Futaki. "Modular Redesign of a Cationic Lytic Peptide To Promote the Endosomal Escape of Biomacromolecules." Angewandte Chemie International Edition 57, no. 39 (August 30, 2018): 12771–74. http://dx.doi.org/10.1002/anie.201807534.

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28

Bechinger, Burkhard. "Peptide-nucleic acid nanostructures for transfection." BioMolecular Concepts 3, no. 3 (June 1, 2012): 283–93. http://dx.doi.org/10.1515/bmc-2011-0067.

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AbstractTo use nucleic acids in biomedical research and medical applications, these highly hydrophilic macromolecules have to be transported through the organism, targeted to specific cell surfaces, and have to cross cellular barriers. To this end, nanosized transfection complexes have been designed and several of them have been successfully tested. Here, the different steps of the transfection process and the particular optimization protocols are reviewed, including the physicochemical properties of such vectors (size, charge, composition), protection in serum, cellular uptake, endosomal escape, and intracellular targeting. The transfection process has been subdivided into separate steps and here special emphasis is given to peptides that have been designed to optimize these steps individually. Finally, complex devices encompassing a multitude of beneficial functionalities for transfection have been developed.

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Ho, Kevin, Cristobal Morfin, and Katarzyna Slowinska. "The Limitations of Collagen/CPP Hybrid Peptides as Carriers for Cancer Drugs to FaDu Cells." Molecules 24, no. 4 (February 14, 2019): 676. http://dx.doi.org/10.3390/molecules24040676.

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The in vitro efficacy of cancer prodrugs varies significantly between malignant cell lines. The most commonly identified problems relate to delivery: uptake mechanism, endosomal entrapment, and drug release. Here we present the study of collagen/cell penetrating hybrid (COL/CPP) peptide carriers intended to deliver paclitaxel to the hypopharyngeal carcinoma (FaDu) cells. Confocal microscopy imaging revealed the surprising response of FaDu cell to COL/CPP in comparison to previously studied cancer cell lines: hybrid peptides that carry both COL and CPP domain adsorb on the FaDu cell surface. While the CPP domain was design to facilitate the cellular uptake, in the case of FaDu cells, it also induced detrimental interactions with the cell membrane. Despite surface adsorption, the colocalization study with endosomal markers EEA1 and LAMP1 reveals that COL/CPP is internalized via endosomal pathway, peptides are able to escape before lysosome formation and release paclitaxel. Therefore, the main obstacle for paclitaxel delivery to FaDu cells appears to be related to cell surface properties. This behavior seems specific to FaDu cells, and could be linked to previously reported overexpression of T5, heparanase splice variants that produces protein lacking enzymatic activity of heparanase. This results in increased concentration of HSPG on FaDu cell surface, and possibly creates a barrier for cellular uptake of highly charged COL/CPP.

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30

Lim, Chaemin, Jin Kook Kang, Woong Roeck Won, June Yong Park, Sang Myung Han, Thi ngoc Le, Jae Chang Kim, Jaewon Her, Yuseon Shin, and Kyung Taek Oh. "Co-delivery of D-(KLAKLAK)2 Peptide and Chlorin e6 using a Liposomal Complex for Synergistic Cancer Therapy." Pharmaceutics 11, no. 6 (June 21, 2019): 293. http://dx.doi.org/10.3390/pharmaceutics11060293.

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Nanotechnology-based photo-chemo combination therapy has been extensively investigated to improve therapeutic outcomes in anticancer treatment. Specifically, with the help of a singlet oxygen generated by the photosensitizer, the endocytosed nanoparticles are allowed to escape from the endosomal compartment, which is currently an obstacle in nanotechnology-based anticancer therapy. In this study, a liposomal complex system (Lipo (Pep, Ce6)), composed of a chlorin e6-conjugated di-block copolymer (PEG-PLL(-g-Ce6)) and a D-(KLAKLAK)2 peptide loading liposome (Lipo (Pep)), was developed and evaluated for its anticancer activity. Due to the membrane lytic ability of the D-(KLAKLAK)2 peptide and the membrane disruptive effect of the singlet oxygen generated from chlorin e6, Lipo (Pep, Ce6) accelerated the disruption of the endosomal compartment, and exhibited strong synergistic anticancer activity in vitro. The prepared liposomal complex system could potentially maximize the efficacy of the nanotechnology-based photo-chemo combination therapy, and can be regarded as a novel, versatile strategy in advanced tumor therapy.

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Luan, Liang, Qingbin Meng, Liang Xu, Zhao Meng, Husheng Yan, and Keliang Liu. "Peptide amphiphiles with multifunctional fragments promoting cellular uptake and endosomal escape as efficient gene vectors." Journal of Materials Chemistry B 3, no. 6 (2015): 1068–78. http://dx.doi.org/10.1039/c4tb01353k.

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Miyoshi, Yuichi, Maho Kadono, Shigetoshi Okazaki, Ayano Nishimura, Mizuki Kitamatsu, Kazunori Watanabe, and Takashi Ohtsuki. "Endosomal Escape of Peptide-Photosensitizer Conjugates Is Affected by Amino Acid Sequences near the Photosensitizer." Bioconjugate Chemistry 31, no. 3 (February 6, 2020): 916–22. http://dx.doi.org/10.1021/acs.bioconjchem.0c00046.

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33

El-Sayed, Ayman, Tomoya Masuda, Ikramy Khalil, Hidetaka Akita, and Hideyoshi Harashima. "Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape." Journal of Controlled Release 138, no. 2 (September 2009): 160–67. http://dx.doi.org/10.1016/j.jconrel.2009.05.018.

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Han, Kai, Qi Lei, Hui-Zhen Jia, Shi-Bo Wang, Wei-Na Yin, Wei-Hai Chen, Si-Xue Cheng, and Xian-Zheng Zhang. "A Tumor Targeted Chimeric Peptide for Synergistic Endosomal Escape and Therapy by Dual-Stage Light Manipulation." Advanced Functional Materials 25, no. 8 (January 13, 2015): 1248–57. http://dx.doi.org/10.1002/adfm.201403190.

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Ayad, Camille, Pierre Libeau, Céline Lacroix-Gimon, Catherine Ladavière, and Bernard Verrier. "LipoParticles: Lipid-Coated PLA Nanoparticles Enhanced In Vitro mRNA Transfection Compared to Liposomes." Pharmaceutics 13, no. 3 (March 12, 2021): 377. http://dx.doi.org/10.3390/pharmaceutics13030377.

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The approval of two mRNA vaccines as urgent prophylactic treatments against Covid-19 made them a realistic alternative to conventional vaccination methods. However, naked mRNA is rapidly degraded by the body and cannot effectively penetrate cells. Vectors capable of addressing these issues while allowing endosomal escape are therefore needed. To date, the most widely used vectors for this purpose have been lipid-based vectors. Thus, we have designed an innovative vector called LipoParticles (LP) consisting of poly(lactic) acid (PLA) nanoparticles coated with a 15/85 mol/mol DSPC/DOTAP lipid membrane. An in vitro investigation was carried out to examine whether the incorporation of a solid core offered added value compared to liposomes alone. To that end, a formulation strategy that we have named particulate layer-by-layer (pLbL) was used. This method permitted the adsorption of nucleic acids on the surface of LP (mainly by means of electrostatic interactions through the addition of LAH4-L1 peptide), allowing both cellular penetration and endosomal escape. After a thorough characterization of size, size distribution, and surface charge— and a complexation assessment of each vector—their transfection capacity and cytotoxicity (on antigenic presenting cells, namely DC2.4, and epithelial HeLa cells) were compared. LP have been shown to be significantly better transfecting agents than liposomes through pLbL formulation on both HeLa and DC 2.4 cells. These data illustrate the added value of a solid particulate core inside a lipid membrane, which is expected to rigidify the final assemblies and makes them less prone to early loss of mRNA. In addition, this assembly promoted not only efficient delivery of mRNA, but also of plasmid DNA, making it a versatile nucleic acid carrier that could be used for various vaccine applications. Finally, if the addition of the LAH4-L1 peptide systematically leads to toxicity of the pLbL formulation on DC 2.4 cells, the optimization of the nucleic acid/LAH4-L1 peptide mass ratio becomes an interesting strategy—essentially reducing the peptide intake to limit its cytotoxicity while maintaining a relevant transfection efficiency.

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Yang, Yujie, Zhen Liu, Hongchao Ma, and Meiwen Cao. "Application of Peptides in Construction of Nonviral Vectors for Gene Delivery." Nanomaterials 12, no. 22 (November 19, 2022): 4076. http://dx.doi.org/10.3390/nano12224076.

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Gene therapy, which aims to cure diseases by knocking out, editing, correcting or compensating abnormal genes, provides new strategies for the treatment of tumors, genetic diseases and other diseases that are closely related to human gene abnormalities. In order to deliver genes efficiently to abnormal sites in vivo to achieve therapeutic effects, a variety of gene vectors have been designed. Among them, peptide-based vectors show superior advantages because of their ease of design, perfect biocompatibility and safety. Rationally designed peptides can carry nucleic acids into cells to perform therapeutic effects by overcoming a series of biological barriers including cellular uptake, endosomal escape, nuclear entrance and so on. Moreover, peptides can also be incorporated into other delivery systems as functional segments. In this review, we referred to the biological barriers for gene delivery in vivo and discussed several kinds of peptide-based nonviral gene vectors developed for overcoming these barriers. These vectors can deliver different types of genetic materials into targeted cells/tissues individually or in combination by having specific structure–function relationships. Based on the general review of peptide-based gene delivery systems, the current challenges and future perspectives in development of peptidic nonviral vectors for clinical applications were also put forward, with the aim of providing guidance towards the rational design and development of such systems.

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Räägel, Helin, Margot Hein, Asko Kriiska, Pille Säälik, Anders Florén, Ülo Langel, and Margus Pooga. "Cell-penetrating peptide secures an efficient endosomal escape of an intact cargo upon a brief photo-induction." Cellular and Molecular Life Sciences 70, no. 24 (July 13, 2013): 4825–39. http://dx.doi.org/10.1007/s00018-013-1416-z.

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Kay, Emma, Rouven Stulz, Cécile Becquart, Jelena Lovric, Carolina Tängemo, Aurélien Thomen, Dženita Baždarević, et al. "NanoSIMS Imaging Reveals the Impact of Ligand-ASO Conjugate Stability on ASO Subcellular Distribution." Pharmaceutics 14, no. 2 (February 21, 2022): 463. http://dx.doi.org/10.3390/pharmaceutics14020463.

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The delivery of antisense oligonucleotides (ASOs) to specific cell types via targeted endocytosis is challenging due to the low cell surface expression of target receptors and inefficient escape of ASOs from the endosomal pathway. Conjugating ASOs to glucagon-like peptide 1 (GLP1) leads to efficient target knockdown, specifically in pancreatic β-cells. It is presumed that ASOs dissociate from GLP1 intracellularly to enable an ASO interaction with its target RNA. It is unknown where or when this happens following GLP1-ASO binding to GLP1R and endocytosis. Here, we use correlative nanoscale secondary ion mass spectroscopy (NanoSIMS) and transmission electron microscopy to explore GLP1-ASO subcellular trafficking in GLP1R overexpressing HEK293 cells. We isotopically label both eGLP1 and ASO, which do not affect the eGLP1-ASO conjugate function. We found that the eGLP1 peptide and ASO are not detected at the same level in the same endosomes, within 30 min of GLP1R-HEK293 cell exposure to eGLP1-ASO. When we utilized different linker chemistry to stabilize the GLP1-ASO conjugate, we observed more ASO located with GLP1 compared to cell incubation with the less stable conjugate. Overall, our work suggests that the ASO separates from GLP1 relatively early in the endocytic pathway, and that linker chemistry might impact the GLP1-ASO function.

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Hao, Xuefang, Qian Li, Hasnain Ali, Syed Saqib Ali Zaidi, Jintang Guo, Xiangkui Ren, Changcan Shi, Shihai Xia, Wencheng Zhang, and Yakai Feng. "POSS-cored and peptide functionalized ternary gene delivery systems with enhanced endosomal escape ability for efficient intracellular delivery of plasmid DNA." Journal of Materials Chemistry B 6, no. 25 (2018): 4251–63. http://dx.doi.org/10.1039/c8tb00786a.

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Li, Margie, Yong Tao, Yilai Shu, Jonathan R. LaRochelle, Angela Steinauer, David Thompson, Alanna Schepartz, Zheng-Yi Chen, and David R. Liu. "Discovery and Characterization of a Peptide That Enhances Endosomal Escape of Delivered Proteins in Vitro and in Vivo." Journal of the American Chemical Society 137, no. 44 (October 30, 2015): 14084–93. http://dx.doi.org/10.1021/jacs.5b05694.

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Niikura, Keisuke, Kenichi Horisawa, and Nobuhide Doi. "A fusogenic peptide from a sea urchin fertilization protein promotes intracellular delivery of biomacromolecules by facilitating endosomal escape." Journal of Controlled Release 212 (August 2015): 85–93. http://dx.doi.org/10.1016/j.jconrel.2015.06.020.

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El-Sayed, Ayman, Tomoya Masuda, Hidetaka Akita, and Hideyoshi Harashima. "Stearylated INF7 Peptide Enhances Endosomal Escape and Gene Expression of PEGylated Nanoparticles both In Vitro and In Vivo." Journal of Pharmaceutical Sciences 101, no. 2 (February 2012): 879–82. http://dx.doi.org/10.1002/jps.22807.

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Wang, Anqi, Yuan Zheng, Wanxin Zhu, Liuxin Yang, Yang Yang, and Jinliang Peng. "Melittin-Based Nano-Delivery Systems for Cancer Therapy." Biomolecules 12, no. 1 (January 12, 2022): 118. http://dx.doi.org/10.3390/biom12010118.

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Melittin (MEL) is a 26-amino acid polypeptide with a variety of pharmacological and toxicological effects, which include strong surface activity on cell lipid membranes, hemolytic activity, and potential anti-tumor properties. However, the clinical application of melittin is restricted due to its severe hemolytic activity. Different nanocarrier systems have been developed to achieve stable loading, side effects shielding, and tumor-targeted delivery, such as liposomes, cationic polymers, lipodisks, etc. In addition, MEL can be modified on nano drugs as a non-selective cytolytic peptide to enhance cellular uptake and endosomal/lysosomal escape. In this review, we discuss recent advances in MEL’s nano-delivery systems and MEL-modified nano drug carriers for cancer therapy.

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Hemmati, Shiva, and Haniyeh Rasekhi Kazerooni. "Polypharmacological Cell-Penetrating Peptides from Venomous Marine Animals Based on Immunomodulating, Antimicrobial, and Anticancer Properties." Marine Drugs 20, no. 12 (December 4, 2022): 763. http://dx.doi.org/10.3390/md20120763.

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Complex pathological diseases, such as cancer, infection, and Alzheimer’s, need to be targeted by multipronged curative. Various omics technologies, with a high rate of data generation, demand artificial intelligence to translate these data into druggable targets. In this study, 82 marine venomous animal species were retrieved, and 3505 cryptic cell-penetrating peptides (CPPs) were identified in their toxins. A total of 279 safe peptides were further analyzed for antimicrobial, anticancer, and immunomodulatory characteristics. Protease-resistant CPPs with endosomal-escape ability in Hydrophis hardwickii, nuclear-localizing peptides in Scorpaena plumieri, and mitochondrial-targeting peptides from Synanceia horrida were suitable for compartmental drug delivery. A broad-spectrum S. horrida-derived antimicrobial peptide with a high binding-affinity to bacterial membranes was an antigen-presenting cell (APC) stimulator that primes cytokine release and naïve T-cell maturation simultaneously. While antibiofilm and wound-healing peptides were detected in Synanceia verrucosa, APC epitopes as universal adjuvants for antiviral vaccination were in Pterois volitans and Conus monile. Conus pennaceus-derived anticancer peptides showed antiangiogenic and IL-2-inducing properties with moderate BBB-permeation and were defined to be a tumor-homing peptide (THP) with the ability to inhibit programmed death ligand-1 (PDL-1). Isoforms of RGD-containing peptides with innate antiangiogenic characteristics were in Conus tessulatus for tumor targeting. Inhibitors of neuropilin-1 in C. pennaceus are proposed for imaging probes or therapeutic delivery. A Conus betulinus cryptic peptide, with BBB-permeation, mitochondrial-targeting, and antioxidant capacity, was a stimulator of anti-inflammatory cytokines and non-inducer of proinflammation proposed for Alzheimer’s. Conclusively, we have considered the dynamic interaction of cells, their microenvironment, and proportional-orchestrating-host- immune pathways by multi-target-directed CPPs resembling single-molecule polypharmacology. This strategy might fill the therapeutic gap in complex resistant disorders and increase the candidates’ clinical-translation chance.

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Higuchi-Takeuchi, Mieko, Takaaki Miyamoto, Choon Pin Foong, Mami Goto, Kumiko Morisaki, and Keiji Numata. "Peptide-Mediated Gene Transfer into Marine Purple Photosynthetic Bacteria." International Journal of Molecular Sciences 21, no. 22 (November 16, 2020): 8625. http://dx.doi.org/10.3390/ijms21228625.

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Use of photosynthetic organisms is one of the sustainable ways to produce high-value products. Marine purple photosynthetic bacteria are one of the research focuses as microbial production hosts. Genetic transformation is indispensable as a biotechnology technique. However, only conjugation has been determined to be an applicable method for the transformation of marine purple photosynthetic bacteria so far. In this study, for the first time, a dual peptide-based transformation method combining cell penetrating peptide (CPP), cationic peptide and Tat-derived peptide (dTat-Sar-EED) (containing D-amino acids of Tat and endosomal escape domain (EED) connected by sarcosine linkers) successfully delivered plasmid DNA into Rhodovulum sulfidophilum, a marine purple photosynthetic bacterium. The plasmid delivery efficiency was greatly improved by dTat-Sar-EED. The concentrations of dTat-Sar-EED, cell growth stage and recovery duration affected the efficiency of plasmid DNA delivery. The delivery was inhibited at 4 °C and by A22, which is an inhibitor of the actin homolog MreB. This suggests that the plasmid DNA delivery occurred via MreB-mediated energy dependent process. Additionally, this peptide-mediated delivery method was also applicable for E. coli cells. Thus, a wide range of bacteria could be genetically transformed by using this novel peptide-based transformation method.

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Ben Djemaa, Sanaa, Katel Hervé-Aubert, Laurie Lajoie, Annarita Falanga, Stefania Galdiero, Steven Nedellec, Martin Soucé, et al. "gH625 Cell-Penetrating Peptide Promotes the Endosomal Escape of Nanovectorized siRNA in a Triple-Negative Breast Cancer Cell Line." Biomacromolecules 20, no. 8 (July 15, 2019): 3076–86. http://dx.doi.org/10.1021/acs.biomac.9b00637.

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Lee, Hyuk, Hongsuk Park, Hyeong Yu, Kun Na, Kyung Oh, and Eun Lee. "Dendritic Cell-Targeted pH-Responsive Extracellular Vesicles for Anticancer Vaccination." Pharmaceutics 11, no. 2 (January 27, 2019): 54. http://dx.doi.org/10.3390/pharmaceutics11020054.

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Immunotherapy can potentially treat cancers on a patient-dependent manner. Most of the efforts expended on anticancer vaccination parallel the efforts expended on prototypical immunization in infectious diseases. In this study, we designed and synthesized pH-responsive extracellular vesicles (EVs) coupled with hyaluronic acid (HA), 3-(diethylamino)propylamine (DEAP), monophosphoryl lipid A (MPLA), and mucin 1 peptide (MUC1), referred to as HDEA@EVAT. HDEA@EVAT potentiated the differentiation and maturation of monocytes into dendritic cells (DCs) and the priming of CD8+ T-cells for cancer therapy. MPLA and HA enabled HDEA@EVAT to interact with the toll-like receptor 4 and the CD44 receptor on DCs, followed by endosomal escape, owing to the protonation of pH-sensitive DEAP on the EV in conjunction with MUC1 release. The MUC1 was then processed and presented to DCs to activate CD8+ T-cells for additional anticancer-related immune reactions. Our findings support the anticancer vaccine activity by which HDEA@EVAT expedites the interaction between DCs and CD8+ T-cells by inducing DC-targeted maturation and by presenting the cancer-associated peptide MUC1.

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Nishimura, Yuya, Koichi Takeda, Ryosuke Ezawa, Jun Ishii, Chiaki Ogino, and Akihiko Kondo. "A display of pH-sensitive fusogenic GALA peptide facilitates endosomal escape from a Bio-nanocapsule via an endocytic uptake pathway." Journal of Nanobiotechnology 12, no. 1 (2014): 11. http://dx.doi.org/10.1186/1477-3155-12-11.

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Sasaki, Kentaro, Kentaro Kogure, Shinji Chaki, Yoshio Nakamura, Rumiko Moriguchi, Hirofumi Hamada, Radostin Danev, Kuniaki Nagayama, Shiroh Futaki, and Hideyoshi Harashima. "An artificial virus-like nano carrier system: enhanced endosomal escape of nanoparticles via synergistic action of pH-sensitive fusogenic peptide derivatives." Analytical and Bioanalytical Chemistry 391, no. 8 (March 20, 2008): 2717–27. http://dx.doi.org/10.1007/s00216-008-2012-1.

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Madani, Fatemeh, Alex Perálvarez-Marín, and Astrid Gräslund. "Liposome Model Systems to Study the Endosomal Escape of Cell-Penetrating Peptides: Transport across Phospholipid Membranes Induced by a Proton Gradient." Journal of Drug Delivery 2011 (December 28, 2011): 1–7. http://dx.doi.org/10.1155/2011/897592.

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Detergent-mediated reconstitution of bacteriorhodopsin (BR) into large unilamellar vesicles (LUVs) was investigated, and the effects were carefully characterized for every step of the procedure. LUVs were prepared by the extrusion method, and their size and stability were examined by dynamic light scattering. BR was incorporated into the LUVs using the detergent-mediated reconstitution method and octyl glucoside (OG) as detergent. The result of measuring pH outside the LUVs suggested that in the presence of light, BR pumps protons from the outside to the inside of the LUVs, creating acidic pH inside the vesicles. LUVs with 20% negatively charged headgroups were used to model endosomes with BR incorporated into the membrane. The fluorescein-labeled cell-penetrating peptide penetratin was entrapped inside these BR-containing LUVs. The light-induced proton pumping activity of BR has allowed us to observe the translocation of fluorescein-labeled penetratin across the vesicle membrane.

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