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• W2164314817 abstract "PEGylation is a well-established technique utilized to overcome the problems related to the therapeutic applications of peptides and proteins. Reasons for the PEGylation of these biological macromolecules include reducing immunogenicity, proteolytic degradation and rapid clearance from blood circulation. Octreotide is an octapeptide analogue of naturally-occurred somatostatin. This peptide has elimination half-life of less than 2 h that requires frequent daily subcutaneous or intravenous administration. To address this issue, octreotide modification was investigated using bis-thiol alkylating PEG reagent. The required bis-thiol alkylating reagent (V) was prepared from commercially available 4-acetyl benzoic acid in five steps. Octreotide disulfide bond was mildly reduced to liberate the two cysteine sulfur atoms followed by bis-alkylation to form PEGylated peptide. The PEG modification process was monitored through the reverse phase HPLC and (1)H-NMR analysis. According to the HPLC chromatograms of PEGylation reaction, the peak with 30 min retention time was identified to be PEG-octreotide. In addition, (1)H-NMR analysis showed a 7.44% degree of PEG substitution." @default.
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• W2164314817 date "2012-01-01" @default.
• W2164314817 modified "2023-09-27" @default.
• W2164314817 title "PEGylation of Octreotide Using an α,β-unsaturated-β'-mono-sulfone Functionalized PEG Reagent." @default.
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• W2164314817 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3813111" @default.
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• W2164314817 hasPublicationYear "2012" @default.
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