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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 02827naa a2200385 4500 | |
| 001 | oai:DiVA.org:su-145857 | |
| 003 | SwePub | |
| 008 | 170823s2017 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1458572 URI |
| 024 | 7 | a https://doi.org/10.1038/NCHEM.27792 DOI |
| 040 | a (SwePub)su | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Akishiba, Misao4 aut |
| 245 | 1 0 | a Cytosolic antibody delivery by lipid-sensitive endosomolytic peptide |
| 264 | 1 | c 2017 |
| 338 | a print2 rdacarrier | |
| 520 | a One of the major obstacles in intracellular targeting using antibodies is their limited release from endosomes into the cytosol. Here we report an approach to deliver proteins, which include antibodies, into cells by using endosomolytic peptides derived from the cationic and membrane-lytic spider venom peptide M-lycotoxin. The delivery peptides were developed by introducing one or two glutamic acid residues into the hydrophobic face. One peptide with the substitution of leucine by glutamic acid (L17E) was shown to enable a marked cytosolic liberation of antibodies (immunoglobulins G (IgGs)) from endosomes. The predominant membrane-perturbation mechanism of this peptide is the preferential disruption of negatively charged membranes (endosomal membranes) over neutral membranes (plasma membranes), and the endosomolytic peptide promotes the uptake by inducing macropinocytosis. The fidelity of this approach was confirmed through the intracellular delivery of a ribosome-inactivation protein (saporin), Cre recombinase and IgG delivery, which resulted in a specific labelling of the cytosolic proteins and subsequent suppression of the glucocorticoid receptor-mediated transcription. We also demonstrate the L17E-mediated cytosolic delivery of exosome-encapsulated proteins. | |
| 650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
| 700 | 1 | a Takeuchi, Toshihide4 aut |
| 700 | 1 | a Kawaguchi, Yoshimasa4 aut |
| 700 | 1 | a Sakamoto, Kentarou4 aut |
| 700 | 1 | a Yu, Hao-Hsin4 aut |
| 700 | 1 | a Nakase, Ikuhiko4 aut |
| 700 | 1 | a Takatani-Nakase, Tomoka4 aut |
| 700 | 1 | a Madani, Fatemehu Stockholms universitet,Institutionen för biokemi och biofysik4 aut |
| 700 | 1 | a Gräslund, Astridu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)astrid |
| 700 | 1 | a Futaki, Shiroh4 aut |
| 710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
| 773 | 0 | t Nature Chemistryg 9:8, s. 751-761q 9:8<751-761x 1755-4330x 1755-4349 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-145857 |
| 856 | 4 8 | u https://doi.org/10.1038/NCHEM.2779 |
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