Structural determination of sildenafil and its analogues in dietary supplements by fast-atom bombardment collision-induced dissociation tandem mass spectrometry

2009 ◽  
Vol 23 (19) ◽  
pp. 3158-3166 ◽  
Author(s):  
Sungho Ahn ◽  
Joo Yeon Hong ◽  
Moo Ki Hong ◽  
Young Pyo Jang ◽  
Myung Sook Oh ◽  
...  
2006 ◽  
Vol 20 (8) ◽  
pp. 1253-1256 ◽  
Author(s):  
Ji Hye Gil ◽  
JungJu Seo ◽  
Kang-Jin Kim ◽  
Jee H. Jung ◽  
Ok-Sang Jung ◽  
...  

2002 ◽  
Vol 16 (22) ◽  
pp. 2089-2093 ◽  
Author(s):  
Jongki Hong ◽  
Young Hwan Kim ◽  
Ji Hye Gil ◽  
Kun Cho ◽  
Jee H. Jung ◽  
...  

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Chia Yen Liew ◽  
Chu-Chun Yen ◽  
Jien-Lian Chen ◽  
Shang-Ting Tsai ◽  
Sujeet Pawar ◽  
...  

AbstractN-linked glycosylation is one of the most important protein post-translational modifications. Despite the importance of N-glycans, the structural determination of N-glycan isomers remains challenging. Here we develop a mass spectrometry method, logically derived sequence tandem mass spectrometry (LODES/MSn), to determine the structures of N-glycan isomers that cannot be determined using conventional mass spectrometry. In LODES/MSn, the sequences of successive collision-induced dissociation are derived from carbohydrate dissociation mechanisms and apply to N-glycans in an ion trap for structural determination. We validate LODES/MSn using synthesized N-glycans and subsequently applied this method to N-glycans extracted from soybean, ovalbumin, and IgY. Our method does not require permethylation, reduction, and labeling of N-glycans, or the mass spectrum databases of oligosaccharides and N-glycan standards. Moreover, it can be applied to all types of N-glycans (high-mannose, hybrid, and complex), as well as the N-glycans degraded from larger N-glycans by any enzyme or acid hydrolysis.


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