Positional Isomers of Monopegylated Interferon α-2a: Isolation, Characterization, and Biological Activity
Clicks: 141
ID: 270730
1997
The success of recombinant interferon alpha in the clinic in part is limited by two properties of the protein: short serum half-life and immunogenicity. To improve these properties, interferon alpha-2a was conjugated with polyethylene glycol (PEG-5000). A homogeneous preparation of monopegylated interferon alpha-2a was subjected to vigorous analytical and activity characterization. A newly developed ampholyte-free chromatofocussing-like cation-exchange HPLC method utilizing a sulfopropyl resin was used to separate the monopegylated protein into 11 species. Peptide mapping, sequencing, and mass spectrometric analyses indicated that these species are positional isomers where each isomer represents a single polymer molecule conjugated to one specific lysine residue. No species with a modification at the amino terminus was observed. All 11 isomers show antiviral and antiproliferative activities in the same range as the parent monopegylated interferon alpha-2a.
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| Authors | Seth P. Monkarsh,Yuemei Ma,Anthony Aglione,Pascal Bailon,Doreen Ciolek,Barabara Debarbieri,Mary C. Graves,Kurt Hollfelder,Hanspeter Michel,Alicia Palleroni,Jill E. Porter,Emil Russoman,Swapan Roy,Yu-Ching E. Pan;Seth P. Monkarsh;Yuemei Ma;Anthony Aglione;Pascal Bailon;Doreen Ciolek;Barabara Debarbieri;Mary C. Graves;Kurt Hollfelder;Hanspeter Michel;Alicia Palleroni;Jill E. Porter;Emil Russoman;Swapan Roy;Yu-Ching E. Pan; |
| Journal | analytical biochemistry |
| Year | 1997 |
| DOI | 10.1006/abio.1997.2128 |
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