Aminomethylpyrene and Tyramine Labels for Oligosaccharides
Format
Poster Presentation
Faculty Mentor Name
Andreas Franz
Faculty Mentor Department
Chemistry
Abstract/Artist Statement
The glycans on glycoproteins play a significant role how these glycoproteins function. However, they are undetectable by chromatography and UV-detection unless they are removed from the glycoprotein and then labeled with a UV-active tag for analysis. In order to overcome this problem a set of standard sugars, were labeled with 3-amino-benzamide (AB), 2-aminomethyl-pyrene (AP), and tyramine (T). The derivatized sugars were chromatographed on a C18 HPLC column and a HYPERCARB column. Collected fractions were then analyzed by Matrix-Assisted Laser Desoption/Ionization (MALDI) mass spectrometry. This was done in order to develop a methodology to label, separate, and characterize the glycans on the glycoprotein beta-lactoglobuline once the glycans had been enzymatically released. The preliminary results of this research showed good chromatographic separation of mixtures. The quality of separation was better for T-labeled sugars than for AP. Labeling with AB was found to be low-yielding. During MALDI-analysis, protonated molecules of sugars derivatized with AP fragmented all the way to the monosaccharide and signs of photo-dimerization between two AP-labels were evident for AP-derivatives.
Location
Virtual
Start Date
25-4-2020 1:00 PM
End Date
25-4-2020 3:00 PM
Aminomethylpyrene and Tyramine Labels for Oligosaccharides
Virtual
The glycans on glycoproteins play a significant role how these glycoproteins function. However, they are undetectable by chromatography and UV-detection unless they are removed from the glycoprotein and then labeled with a UV-active tag for analysis. In order to overcome this problem a set of standard sugars, were labeled with 3-amino-benzamide (AB), 2-aminomethyl-pyrene (AP), and tyramine (T). The derivatized sugars were chromatographed on a C18 HPLC column and a HYPERCARB column. Collected fractions were then analyzed by Matrix-Assisted Laser Desoption/Ionization (MALDI) mass spectrometry. This was done in order to develop a methodology to label, separate, and characterize the glycans on the glycoprotein beta-lactoglobuline once the glycans had been enzymatically released. The preliminary results of this research showed good chromatographic separation of mixtures. The quality of separation was better for T-labeled sugars than for AP. Labeling with AB was found to be low-yielding. During MALDI-analysis, protonated molecules of sugars derivatized with AP fragmented all the way to the monosaccharide and signs of photo-dimerization between two AP-labels were evident for AP-derivatives.
