Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이은규 | - |
dc.date.accessioned | 2019-07-15T04:52:07Z | - |
dc.date.available | 2019-07-15T04:52:07Z | - |
dc.date.issued | 2007-11 | - |
dc.identifier.citation | BIOCONJUGATE CHEMISTRY, v. 18, No. 6, Page. 1728-1734 | en_US |
dc.identifier.issn | 1043-1802 | - |
dc.identifier.uri | https://pubs.acs.org/doi/abs/10.1021/bc060245m | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/107368 | - |
dc.description.abstract | 'Solid-phase' PEGylation, in which a conjugation reaction attaches proteins to a solid matrix, has distinct advantages over the conventional, solution-phase process. We report a case study in which recombinant interferon (rhIFN) alpha-2a was adsorbed to a cation-exchange resin and PEGylated at the N-terminus by 5, 10, and 20 kDa mPEG aldehydes through reductive alkylation. After PEGylation, a salt gradient elution efficiently purified the mono-PEGylate of unwanted species such as unmodified IFN and unreacted PEG. Mono-PEGylation and purification were integrated into a single, chromatographic step. Depending on the molecular weight of the mPEG aldehyde, the mono-PEGylation yield ranged from 50 to 65%. Major problems associated with the solution-phase process such as random or uncontrollable multi-PEGylation and post-PEGylation purification difficulties were overcome. N-terminus sequencing and MALDI-TOF mass spectrophometry confirmed that the PEG molecule was conjugated only to the N-terminus. A cell proliferation study indicated reduced antiviral activity of the mono-PEGylate compared to that of the unmodified IFN. As higher molecular weight PEG was conjugated, in vitro bioactivity and antibody binding activity, as measured by a surface plasmon. resonance biosensor, decreased. Nevertheless, trypsin resistance and thermal stability were considerably improved | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | AMER CHEMICAL SOC | en_US |
dc.title | Solid-Phase PEGylation of Recombinant Interferon α-2a for Site-Specific Modification: Process Performance, Characterization, and in Vitro Bioactivity | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1021/bc060245m | - |
dc.relation.journal | BIOCONJUGATE CHEMISTRY | - |
dc.contributor.googleauthor | Lee, Byung Kook | - |
dc.contributor.googleauthor | Kwon, Jin Sook | - |
dc.contributor.googleauthor | Kim, Hyung Jin | - |
dc.contributor.googleauthor | Yamamoto, Shuichi | - |
dc.contributor.googleauthor | Lee, E. K. | - |
dc.relation.code | 2007201260 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF ENGINEERING SCIENCES[E] | - |
dc.sector.department | DEPARTMENT OF BIONANO ENGINEERING | - |
dc.identifier.pid | eklee | - |
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