Abstract
[structure: see text] Semisynthesis of an active tetraphosphorylated analogue of the Type I TGFbeta receptor is reported. An efficient native chemical ligation protocol was developed to link a tetraphosphopeptide and a recombinant receptor fragment. Synthesis of the peptide alpha-thioester on a 4-sulfamylbutyryl resin was optimized following the characterization of a major side reaction and subsequent substitution of norleucine for methionine in the peptide sequence. These optimized protocols will be applicable to the semisynthesis of related protein kinases.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Activin Receptors, Type I / chemical synthesis*
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Amino Acid Motifs
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Electrophoresis, Polyacrylamide Gel
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Phosphoproteins / chemical synthesis
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Phosphorylation
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Protein Serine-Threonine Kinases
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Receptor, Transforming Growth Factor-beta Type I
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Receptors, Transforming Growth Factor beta
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Resins, Synthetic
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Serine
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Threonine
Substances
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Phosphoproteins
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Receptors, Transforming Growth Factor beta
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Resins, Synthetic
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Threonine
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Serine
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Protein Serine-Threonine Kinases
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Activin Receptors, Type I
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Receptor, Transforming Growth Factor-beta Type I