Selected article for: "heparin affinity and splicing correction"
Author: Abes, Rachida; Moulton, Hong M.; Clair, Philippe; Yang, Sung-Tae; Abes, Said; Melikov, Kamran; Prevot, Paul; Youngblood, Derek S.; Iversen, Patrick L.; Chernomordik, Leonid V.; Lebleu, Bernard
Title: Delivery of steric block morpholino oligomers by (R-X-R)(4) peptides: structure–activity studies
  • Document date: 2008_9_16
    • ID: 5j496cx0_39
    Snippet: Since the hydrophobicity of the linker appeared to influence splicing correction efficiency, we have compared a series of PMO conjugates (compounds 8-11 in Figure 2A ) with the same spacing (a 6-carbon atom spacer as in (R-Ahx-R) 4 -PMO) but with varying sidechain hydrophobicities. Figure 1C . 5, (R-Ahx-R) 4 -PMO; 13, (r-Ahx-R) 4 -PMO. (C) Hydrophobicity chromatography. Samples were treated and data were processed as described in the legend of Fi.....
    Document: Since the hydrophobicity of the linker appeared to influence splicing correction efficiency, we have compared a series of PMO conjugates (compounds 8-11 in Figure 2A ) with the same spacing (a 6-carbon atom spacer as in (R-Ahx-R) 4 -PMO) but with varying sidechain hydrophobicities. Figure 1C . 5, (R-Ahx-R) 4 -PMO; 13, (r-Ahx-R) 4 -PMO. (C) Hydrophobicity chromatography. Samples were treated and data were processed as described in the legend of Figure 2B . (D) Heparin affinity chromatography. Samples were treated and data were processed as described in the legend of Figure 1B . ÃÃÃ and ÃÃ Indicate statistically significant differences; NS indicates that the difference is not statistically significant.

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