Sulfonation of arginine residues as side reaction in Fmoc‐peptide synthesis

作者：Annette G. Beck‐Sickinger, Gerd Schnorrenberg, Jörg Wolfgang Metzger, Günther Jung · 发表于：International journal of peptide & protein research · 年份：1991 · DOI：10.1111/j.1399-3011.1991.tb01405.x · 被引用次数：31 · 研究领域：Chemical Synthesis and Analysis、Neuropeptides and Animal Physiology、Mass Spectrometry Techniques and Applications

Several arginine-rich peptides containing the C-terminus of neuropeptide Y (NPY) were prepared by solid phase peptide synthesis using Fmoc chemistry and cleaved from the resin with trifluoroacetic acid (TFA). The products were characterized by fast atom bombardment-MS, LC-thermospray-MS, ion spray-MS/MS, and Edman degradation. The side products could be identified as peptides with sulfonated arginine residues resulting from an unexpected cleavage of Mtr or Pmc protecting groups. The degree of sulfonation depended on the choice and composition of the cleavage solution. Several scavenger mixtures were used and a mixture of thioanisole/thiocresol was found to be the most efficient for suppressing sulfonation. Furthermore treatment with the enzyme arylsulfate-sulfohydrolase desulfonated the peptides yielding the correct sequence.