English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Interferon-α2b (IFN-α2b) is used as a therapeutic agent against various types of cancer. In the current research, modified forms of human INF-α2b were produced to investigate the effect of amino acid substitutions on binding to the interferon receptor and antiproliferative activity. The resulting modified human IFN-α2b proteins were PEGylated to increase their  in vivo  circulation half-life. N-terminal PEGylation was performed using mPEG-propionaldehyde succinate (20 and 40 kDa). As a result of these modifications, IFN-α2b with modification R(23)H achieved IC 50  at 0.062 ng as compared to wild type IFN-α2b (0.125 ng). PEGylation of IFN-α2b and its modified forms resulted in an increase in hydrodynamic volume and serum retention time (up to 62 h) compared to wild type IFN-α2b (4 h). However, the antiproliferative activities of PEGylated IFN against HepG2 cell line were decreased (up to 4.7%) with an increase in PEGylated IFN-α2b size as compared to the wild type.

PEGylation of human interferon-α2b with modified amino acids increases circulation half-life and antiproliferative activity