Related Experiment Video
Updated: Jul 8, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
Published on: May 30, 2025
A sulfated, phosphorylated 7 kDa secreted peptide characterized by direct analysis of cell culture media
Steven W Taylor1, Chengzao Sun, Amy Hsieh
1Amylin Pharmaceuticals, Inc., 9360 Towne Centre Drive, San Diego, California 92121, USA. staylor@amylin.com
Abstract:
An unusual sulfotyrosine-, phosphoserine-containing motif was mapped on a differentially post-translationally modified 60 residue antimicrobial neuroendocrine peptide called chrombacin. The study was performed by high resolution FT MS using complementary fragmentation techniques. The peptide was analyzed at low levels directly from cell culture media in contrast to previous reports that required extensive purification and proteolytic digestion. The sulfation site was not previously described nor predicted by informatic analysis of the peptide's precursor sequence.

