Probing the stability of nonglycosylated wild-type erythropoietin protein via reiterative alanine ligations Journal Article


Authors: Brailsford, J. A.; Danishefsky, S. J.
Article Title: Probing the stability of nonglycosylated wild-type erythropoietin protein via reiterative alanine ligations
Abstract: Nonglycosylated erythropoietin bearing acetamidomethyl protecting groups at the cysteine residues has been synthesized via chemical methods. Alanine ligation was used to assemble four peptide fragments, themselves prepared by solid phase peptide synthesis. This work outlines a route for the synthesis of homogeneous glycosylated erythropoietin.
Keywords: controlled study; erythropoietin; protein stability; wild type; amino acid sequence; molecular sequence data; peptide fragments; peptide fragment; glycosylation; molecular structure; alanine; protein structure; protein structure, secondary; models, chemical; carbohydrate sequence; desulfurization; cysteine; peptide synthesis; oligosaccharides; solid phase synthesis; methyl group; protein glycosylation; solid phase peptide synthesis
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 109
Issue: 19
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2012-05-08
Start Page: 7196
End Page: 7201
Language: English
DOI: 10.1073/pnas.1202762109
PROVIDER: scopus
PMCID: PMC3358843
PUBMED: 22499784
DOI/URL:
Notes: --- - "Cited By (since 1996): 1" - "Export Date: 4 June 2012" - "CODEN: PNASA" - "Source: Scopus"
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