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Sökning: L773:1940 6029 > Stockholms universitet

  • Resultat 1-10 av 10
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1.
  • Cerrato, C. P., et al. (författare)
  • Mitochondrial Targeting Probes, Drug Conjugates, and Gene Therapeutics
  • 2022
  • Ingår i: Cell Penetrating Peptides. - New York, NY : Springer Nature. ; 2383, s. 429-446
  • Bokkapitel (refereegranskat)abstract
    • Mitochondria represent an important drug target for many phatology, including neurodegeneration, metabolic disease, heart failure, ischemia-reperfusion injury, and cancer. Mitochondrial dysfunctions are caused by mutation in mitochondrial DNA or in nuclear genes encoding mitochondrial proteins. Cell-penetrating peptides (CPPs) have been employed to overcome biological barriers, target this organelle, and therapeuticaly restore mitochondrial functions. Here, we describe recent methods used to deliver oligonucleotides targeting mitochondrial protein by using mitochondrial penetrating peptides. In particular, we highlight recent advances of formulated peptides/oligonucleotides nanocomplexes as a proof-of-principle for pharmaceutical form of peptide-based therapeutics.
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2.
  • Dash-Wagh, Suvarna, et al. (författare)
  • PepFect6 Mediated SiRNA Delivery into Organotypic Cultures
  • 2016
  • Ingår i: SiRNA Delivery Methods. - TOTOWA : HUMANA PRESS INC. - 9781493931125 - 9781493931118 ; 1364, s. 27-35
  • Bokkapitel (refereegranskat)abstract
    • Gene silencing by small interfering RNA (SiRNA) is an attractive therapeutic approach for pathological disorders that targets a specific gene. However, its applications are limited, as naked RNA is rapidly degraded by RNases and is inadequately internalized by the target cells in the body. Several viral and non-viral vectors have been described to improve the delivery of SiRNAs both in cultured cells as well as in vivo. Increasing evidence suggests that cell-penetrating peptides (CPPs) are an efficient, non-cytotoxic tool for intracellular delivery of SiRNA. Recently, a new peptide, PepFect6 (PF6), based system has been described for efficient SiRNA delivery in various cell types. PF6 is an amphipathic stearyl-TP10 peptide carrying a pH titratable trifluoromethylquinoline moiety that facilitate endosomal release. PF6 forms stable non-covalent complexes with SiRNA. Upon internalization, the complexes rapidly escape the endosomal compartment, resulting in robust RNA interference (RNAi) responses. This chapter describes a protocol to use the PF6-nanoparticle technology for SiRNA delivery into organotypic cultures of the inner ear i.e., cochlea. We also highlight different critical points in the peptide/SiRNA complex preparation, transfection and in analyzing the efficacy of PF6-SiRNA associated RNAi response.
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3.
  • EL Andaloussi, Samir, et al. (författare)
  • Cell-penetrating peptides-based strategies for the delivery of splice redirecting antisense oligonucleotides
  • 2011
  • Ingår i: Therapeutic Oligonucleotides. - New York : Humana Press. ; 764, s. 75-89
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
    • Progress in our understanding of the molecular pathogenesis of human malignancies has provided therapeutic targets amenable to oligonucleotide (ON)-based strategies. Antisense ON-mediated splicing regulation in particular offers promising prospects since the majority of human genes undergo alternative splicing and since splicing defects have been found in many diseases. However, their implementation has been hampered so far by the poor bioavailability of nucleic acids-based drugs. Cell-penetrating peptides (CPPs) now appear as promising non-viral delivery vector for non-permeant biomolecules. We describe here new CPPs allowing the delivery of splice redirecting steric-block ON using either chemical conjugation or non-covalent complexation. We also describe a convenient and robust splice redirecting assay which allows the quantitative assessment of ON nuclear delivery.
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4.
  • Gräslund, Astrid, et al. (författare)
  • Testing membrane interactions of CPPs
  • 2011
  • Ingår i: Methods in molecular biology (Clifton, N.J.). - Totowa, NJ : Humana Press. - 1940-6029. ; 683, s. 33-40
  • Tidskriftsartikel (refereegranskat)abstract
    • The chapter deals with some biophysical methods used for investigating CPP-induced changes in membrane properties by spectroscopy methods such as fluorescence or NMR and methods used for probing CPP-induced leakage in membranes. Some useful model systems for biomembranes are described. These include large unilamellar phospholipid vesicles (LUVs) of well-defined size (diameter typically 100 nm). A protocol for the preparation of such vesicles is included. The leakage studies make use of LUVs with entrapped dye molecules. The NMR studies make use of mixed micelles (bicelles) as a membrane mimetic system, which can be oriented in the magnetic field of the spectrometer.
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5.
  • Johansson, Henrik J., et al. (författare)
  • Mimicry of protein function with cell-penetrating peptides
  • 2011
  • Ingår i: Cell-penetrating peptides. - Totowa, NJ : Humana Press. - 9781607619185 - 9781607619192 ; 683, s. 233-47
  • Bokkapitel (refereegranskat)abstract
    • Proteins are essential components of cellular processes inside cells, and their interactions between each other and with genes are important for the normal physiological functioning of cells as well as for disease states. Modulating protein interactions by different means can potentially control these interactions and restore normal function to diseased cells. The ways to do so are multiple, and such efforts often begin with knowledge of potential target proteins in order to devise mediators that retain the function of the original protein, i.e., mimic the protein functions. An alternative strategy is to utilize protein mimics to inhibit target proteins rather than restoring the activity of a protein. The vast majority of protein ­mimics exploited to date have been designed to inhibit the activity of oncogenes or activate tumor suppressors for the purpose of tumor therapy. These protein mimics are usually based on small organic compounds or peptides, derived from interaction surfaces of the proteins, and in some cases, full proteins have been exploited. Although peptides and proteins are naturally highly specific and efficient inside cells, they suffer from low bioavailability resulting from their inability to enter cells. One strategy increasingly employed to facilitate the internalization of peptides and proteins has been to chemically conjugate them to cell-penetrating peptides (CPP) or to recombinantly express protein–CPP fusion constructs.This chapter provides an overview of some of the aspects of perturbing and mimicking protein interactions using peptides and proteins and CPP as transport vectors.
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6.
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7.
  • Mäler, Lena, et al. (författare)
  • NMR studies of three-dimensional structure and positioning of CPPs in membrane model systems
  • 2011
  • Ingår i: Methods in molecular biology (Clifton, N.J.). - Totowa, NJ : Humana Press. - 1940-6029. ; 683, s. 57-67
  • Tidskriftsartikel (refereegranskat)abstract
    • CPPs are generally short cationic peptides that have the capability to interact directly with membranes. Most CPPs attain a three-dimensional structure when interacting with bilayers, while they are more or less unstructured in aqueous solution. To understand the relationship between structure and the effect that CPPs have on membranes, it is of great importance to investigate CPPs with atomic resolution in a suitable membrane model. Nuclear magnetic resonance (NMR) is an excellent technique both for studying solution structures of peptides as well as for investigating their location within a model bilayer. This chapter outlines protocols for producing model membrane systems for NMR investigations as well as the basic NMR tools for determining the three-dimensional structure of CPPs and for investigating the details in lipid-peptide interactions, i.e., the localization of the CPP in the bilayer.
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8.
  • Sjölinder, Hong, et al. (författare)
  • In vivo imaging of meningococcal disease dynamics.
  • 2012
  • Ingår i: Methods in molecular biology (Clifton, N.J.). - Totowa, NJ : Humana Press. - 1940-6029. ; 799, s. 153-68
  • Tidskriftsartikel (refereegranskat)abstract
    • Neisseria meningitidis is a human specific organism that causes severe sepsis and/or meningitis with high mortality. The disease scenario is rapid and much remains unknown about the disease process and host-pathogen interaction. In this chapter, we describe a protocol for generating a bioluminescently labeled N. meningitidis strain in order to advance our understanding of meningococcal disease progression. We also describe how in vivo bioluminescence imaging (BLI) can be used to observe novel features of the disease dynamics during meningococcal infection.
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9.
  • Teixeira, Pedro F., et al. (författare)
  • A Flowchart to Analyze Protease Activity in Plant Mitochondria
  • 2015
  • Ingår i: Plant Mitochondria. - New York, NY : Springer-Verlag New York. - 9781493926398 - 9781493926381 ; 1305, s. 123-30
  • Bokkapitel (refereegranskat)abstract
    • Proteases are one of the most abundant classes of enzymes and are involved in a plethora of biological processes in many cellular compartments, including the mitochondria. To understand the role of proteases is essential to determine their substrate repertoire, preferably in an in vivo setting. In this chapter we describe general guidelines to analyze protease activity using several strategies, from in-gel analysis to mass spectrometry mapping of the cleavage site(s) and fluorogenic probes that can easily be used in vivo. To exemplify this flowchart, we used the recently characterized organellar oligopeptidase of Arabidopsis (Arabidopsis thaliana), an enzyme that takes part in degradation of short peptides within mitochondria and chloroplasts.
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10.
  • Vukojevic, Vladana, et al. (författare)
  • Fluorescence Imaging with Single-Molecule Sensitivity and Fluorescence Correlation Spectroscopy of Cell-Penetrating Neuropeptides
  • 2011
  • Ingår i: Neuropeptides. - Totowa, NJ : Humana Press. - 9781617793097 ; 789, s. 147-70
  • Bokkapitel (refereegranskat)abstract
    • Neuropeptide plasma membrane interactions in the absence of a corresponding specific receptor may result in neuropeptide translocation into the cell. Trans location across the plasma membrane may represent a previously unknown mechanism by which neuropeptides can signal information to the cell interior. We introduce here two complementary optical methods with single-molecule sensitivity, fluorescence imaging with avalanche photodiode detectors (APD imaging) and fluorescence correlation spectroscopy (FCS), and demonstrate how they may be applied for the analysis of neuropeptide ability to penetrate into live cells in real time. APD imaging enables us to visualize fluorescently labeled neuropeptide molecules at very low, physiologically relevant concentrations, whereas FCS enables us to characterize quantitatively their concentration and diffusion properties in different cellular compartments. Application of these methodologies for the analysis of the endogenous opioid peptide dynorphin A (Dyn A), a ligand for the kappa-opioid receptor (KOP), demonstrated that this neuropeptide may translocate across the plasma membrane of living cells and enter the cellular interior without binding to its cognate receptor.
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