Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetr...
Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability
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London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Amphipathic arginine-rich peptide, A2-17, exhibits moderate perturbation of lipid membranes and the highest cell penetration among its structural isomers. We investigated the direct cell-membrane penetration mechanism of the A2-17 peptide while focusing on structural flexibility. We designed conformationally constrained versions of A2-17, stapled (...
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Full title
Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability
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TN_cdi_doaj_primary_oai_doaj_org_article_b8893099f948499b954ee0db0b116037
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b8893099f948499b954ee0db0b116037
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ISSN
2045-2322
E-ISSN
2045-2322
DOI
10.1038/s41598-023-46754-0
