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• W2912638027 abstract "Interactions of chemically modified nucleic acid therapeutics with plasma proteins play an important role in facilitating distribution from the injection site to peripheral tissues by reducing renal clearance. Despite the importance of these interactions, analytical methods that can characterize binding constants with individual plasma proteins in a reliable and high throughput manner are not easily available. We developed a fluorescence polarization (FP) based assay and measured binding constants for the 25 most abundant human plasma proteins with phosphorothioate (PS) modified antisense oligonucleotides (ASOs). We evaluated the influence of sequence, sugar modifications, and PS content on ASO interactions with several abundant human plasma proteins and determined the effect of salt and pH on these interactions. PS ASOs were found to associate predominantly with albumin and histidine-rich glycoprotein (HRG) in mouse and human plasma by size-exclusion chromatography. In contrast, PS ASOs associate predominantly with HRG in monkey plasma because of higher concentrations of this protein in monkeys. Finally, plasma proteins capable of binding PS ASOs in human plasma were confirmed by employing affinity chromatography and proteomics. Our results indicate distinct differences in contributions from the PS backbone, nucleobase composition and oligonucleotide flexibility to protein binding." @default.
• W2912638027 created "2019-02-21" @default.
• W2912638027 creator A5009098620 @default.
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• W2912638027 date "2018-12-19" @default.
• W2912638027 modified "2023-10-12" @default.
• W2912638027 title "Characterization of the interactions of chemically-modified therapeutic nucleic acids with plasma proteins using a fluorescence polarization assay" @default.
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• W2912638027 doi "https://doi.org/10.1093/nar/gky1260" @default.
• W2912638027 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6379706" @default.
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• W2912638027 hasPublicationYear "2018" @default.
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