Publications by authors named "Dae Bong Moon"

A hyperglycosylated recombinant human interferon-β (rhIFN-β) R27T mutant was established to improve relapsing-remitting multiple sclerosis (RRMS) in our previous study. We focused on the stability of the R27T mutant throughout its production lifetime, including culture, purification, and storage before formulation prior to clinical use. Herein, we address the stability of this protein during optimized culture and purification processes.

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We previously developed a biobetter version of rhIFN-β (R27T) that possesses an additional glycosylation site compared with rhIFN-β 1a. Herein, we characterized N-glycosylation heterogeneity of R27T, which includes both N-glycan site occupancy heterogeneity (macro-heterogeneity) and complexity of carbohydrate moieties (micro-heterogeneity). N-glycan site occupancy manifested as distinct differences in size and isoelectric point.

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Background: Interleukin-32 (IL-32) has been associated with various diseases. Previous studies have shown that IL-32 inhibited the development of several tumors. However, the role of IL-32γ, an isotype of IL-32, in skin carcinogenesis remains unknown.

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The low expression of tissue inhibitor of metalloproteinase 3 (TIMP-3) is important in inflammatory responses. Therefore, inhibition of TIMP-3 may promote tumor development. Our study showed that expression of TIMP-3 was elevated in lL-32γ mice lung tissues.

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Neuroinflammation is implicated for dopaminergic neurodegeneration. Sulfur compounds extracted from garlic have been shown to have anti-inflammatory properties. Previously, we have investigated that thiacremonone, a sulfur compound isolated from garlic has anti-inflammatory effects on several inflammatory disease models.

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Article Synopsis
  • - Protein modifications in recombinant pharmaceuticals can lead to decreased efficacy, changes in bioavailability, and increased antigenicity, making it crucial to monitor these modifications for quality assurance.
  • - The study focused on erythropoietin (EPO) and its receptor, identifying specific amino acids involved in their interaction and noting two types of modifications in the recombinant human EPO (rHu-EPO BRP) preparation.
  • - A UPLC/Q-TOF MS method was employed to analyze the extent of modifications, revealing that oxidation occurred at Met54 (3.0%) and deamidation at Asn47 (2.9%) and Asn147 (4.8%).
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