FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4322620277> ?p ?o ?g. }

• W4322620277 endingPage "105" @default.
• W4322620277 startingPage "95" @default.
• W4322620277 abstract "Introduction. Highly glycosylated proteins are the most abundant class of modern biopharmaceuticals. A majority of such therapeuticals produced by Russian biopharmaceutical companies is biosimilars. The foundation of biosimilar manufacturing is analytical assessment of structure equivalence to an original molecule. Fc-fusions present a challenge due to their structural properties. The only biosimilar of this kind registered in Russia is etanercept – a fusion of tumor necrosis factor receptor α and Fc-fragment of IgG1. Existing approaches widely used in protein analysis do not allow accurate and reliable description of glycoylation of these proteins. Development of new approaches and principles of such analysis is necessary, as the changes in biosimilar’s molecular structure can seriously affect its efficacy and safety. Aim. Development of double proteolysis approaches for glycopeptide mapping of Fc-fusion protein etanercept using Arg-C protease. Materials and methods. Etanercept was subjected to enzymatic hydrolysis using trypsin in combination with Arg-C or Asp-N. The resulting peptides were analyzed using HPLC-MS system Xevo G2-XS QTOF (Waters Corporation, USA). The conformation of glycan structure was performed via analysis of fragment spectra of glycopeptides, acquired with high collision energy mode (MS E ). UNIFI (version 1.8) with biopharmasuetical assessment setting (Waters Corporation, USA) was used to analyze the peptide maps. Results and discussion. It was found that using the combination of trypsin with protease Arg-C leads to reliable results Using the developed approach we successfully determined the majority of O-glycosylation sites and types of O-glycans. It was shown that for an effective O-glycopeptide maping N-deglycosylation stage is required. Most abundant N-glycan structures were identified for each of three N-glycosylation sites (N149, N171, N317). It was determined, that the combination of trypsin with Arg-C allows identification of three-antenna forms despite the presence of O-glycosylation site on the analyzed peptide. General N-glycosylation profile shows comparability of results for both approaches. Conclusion. As a result of this research we developed glycopeptide mapping approaches in which a combination of proteases is used. Using these methods sites of N- and O-glycosilation and glycofoms of etanercept were accurately and reproducibly determined. Developed procedures can be applied to other types of Fc-fusion proteins, making it of broader appeal and benefit to the overall biopharmaceutical industry. These approaches provide comprehensive information useful for structure-function studies and of potential value for product comparability measurements and possibly even future manufacturing control strategies." @default.
• W4322620277 created "2023-03-01" @default.
• W4322620277 creator A5027496241 @default.
• W4322620277 creator A5052825172 @default.
• W4322620277 creator A5066958563 @default.
• W4322620277 creator A5071199767 @default.
• W4322620277 creator A5071390552 @default.
• W4322620277 date "2023-02-27" @default.
• W4322620277 modified "2023-10-01" @default.
• W4322620277 title "Double Proteolysis for N- and O-glycan Analysis of Fc-fusion Protein Etanercept" @default.
• W4322620277 cites W1991787417 @default.
• W4322620277 cites W1997106678 @default.
• W4322620277 cites W2003021861 @default.
• W4322620277 cites W2028019069 @default.
• W4322620277 cites W2030857400 @default.
• W4322620277 cites W2030899178 @default.
• W4322620277 cites W2044791218 @default.
• W4322620277 cites W2061234311 @default.
• W4322620277 cites W2073890435 @default.
• W4322620277 cites W2130917751 @default.
• W4322620277 cites W2146223797 @default.
• W4322620277 cites W2156979594 @default.
• W4322620277 cites W2318113264 @default.
• W4322620277 cites W2329169489 @default.
• W4322620277 cites W2336127483 @default.
• W4322620277 cites W2343251287 @default.
• W4322620277 cites W2409718956 @default.
• W4322620277 cites W2529379373 @default.
• W4322620277 cites W2607809077 @default.
• W4322620277 cites W2793655673 @default.
• W4322620277 cites W2805894928 @default.
• W4322620277 cites W2901943083 @default.
• W4322620277 cites W2904971004 @default.
• W4322620277 cites W2965860469 @default.
• W4322620277 cites W3012447627 @default.
• W4322620277 cites W3085956438 @default.
• W4322620277 cites W3119024742 @default.
• W4322620277 cites W4285241625 @default.
• W4322620277 doi "https://doi.org/10.33380/2305-2066-2023-12-1-95-105" @default.
• W4322620277 hasPublicationYear "2023" @default.
• W4322620277 type Work @default.
• W4322620277 citedByCount "0" @default.
• W4322620277 crossrefType "journal-article" @default.
• W4322620277 hasAuthorship W4322620277A5027496241 @default.
• W4322620277 hasAuthorship W4322620277A5052825172 @default.
• W4322620277 hasAuthorship W4322620277A5066958563 @default.
• W4322620277 hasAuthorship W4322620277A5071199767 @default.
• W4322620277 hasAuthorship W4322620277A5071390552 @default.
• W4322620277 hasBestOaLocation W43226202771 @default.
• W4322620277 hasConcept C108625454 @default.
• W4322620277 hasConcept C150903083 @default.
• W4322620277 hasConcept C181199279 @default.
• W4322620277 hasConcept C185592680 @default.
• W4322620277 hasConcept C206212055 @default.
• W4322620277 hasConcept C2776714187 @default.
• W4322620277 hasConcept C2777313579 @default.
• W4322620277 hasConcept C2780340462 @default.
• W4322620277 hasConcept C2781047461 @default.
• W4322620277 hasConcept C2781307694 @default.
• W4322620277 hasConcept C55493867 @default.
• W4322620277 hasConcept C59491497 @default.
• W4322620277 hasConcept C70721500 @default.
• W4322620277 hasConcept C86803240 @default.
• W4322620277 hasConceptScore W4322620277C108625454 @default.
• W4322620277 hasConceptScore W4322620277C150903083 @default.
• W4322620277 hasConceptScore W4322620277C181199279 @default.
• W4322620277 hasConceptScore W4322620277C185592680 @default.
• W4322620277 hasConceptScore W4322620277C206212055 @default.
• W4322620277 hasConceptScore W4322620277C2776714187 @default.
• W4322620277 hasConceptScore W4322620277C2777313579 @default.
• W4322620277 hasConceptScore W4322620277C2780340462 @default.
• W4322620277 hasConceptScore W4322620277C2781047461 @default.
• W4322620277 hasConceptScore W4322620277C2781307694 @default.
• W4322620277 hasConceptScore W4322620277C55493867 @default.
• W4322620277 hasConceptScore W4322620277C59491497 @default.
• W4322620277 hasConceptScore W4322620277C70721500 @default.
• W4322620277 hasConceptScore W4322620277C86803240 @default.
• W4322620277 hasIssue "1" @default.
• W4322620277 hasLocation W43226202771 @default.
• W4322620277 hasOpenAccess W4322620277 @default.
• W4322620277 hasPrimaryLocation W43226202771 @default.
• W4322620277 hasRelatedWork W2007116319 @default.
• W4322620277 hasRelatedWork W2030857400 @default.
• W4322620277 hasRelatedWork W2221488325 @default.
• W4322620277 hasRelatedWork W2326801645 @default.
• W4322620277 hasRelatedWork W2612333040 @default.
• W4322620277 hasRelatedWork W2756221472 @default.
• W4322620277 hasRelatedWork W2885484520 @default.
• W4322620277 hasRelatedWork W3038018119 @default.
• W4322620277 hasRelatedWork W4289517913 @default.
• W4322620277 hasRelatedWork W4382395821 @default.
• W4322620277 hasVolume "12" @default.
• W4322620277 isParatext "false" @default.
• W4322620277 isRetracted "false" @default.
• W4322620277 workType "article" @default.