Advanced Glycomics and Glycoproteomics Methods
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Texas Tech University
Dr. Yehia Mechref received his BS in Chemistry at the American University of Beirut, Beirut, Lebanon, and a PhD with an…
Glycosylation of proteins is the most common modification that modulates the biological functions of vital biomolecules. Glycosylation of proteins involves the addition and trimming of several monosaccharides controlled by actions of numerous transferases and exoglycosidases. The glycosylation process's complexity results in highly diverse glycan structures and unique characteristics of cells, tissues, and organisms. Mass Spectrometry-based glycomics and glycoproteomics continue to be highly dynamic and exciting research areas due to the need to comprehensively understand the biological attributes of protein glycosylation in many critical biological functions. Moreover, aberrant glycosylation has been recognized for decades as the trait of many mammalian diseases, including osteoarthritis, cystic fibrosis, and cancer. Although glycoproteins and glycopeptides have attracted significant interests for years, a comprehensive characterization of protein glycosylation microheterogeneity continues to be an arduous task, complicated by the presence of multiple sites occupied by a large number of isomeric structures. Additionally, isomeric separation of glycans and glycopeptides remains a daunting analytical task. Therefore, the development of analytical methods, sensitive and efficient in characterizing the diverse glycan structures, associated with proteins is still in demand and highly desired.
Analytical methods employing cutting-edge techniques such as mass spectrometry (MS), chromatography, and capillary electrophoresis, have been developed to characterize the glycan moieties of glycoproteins unequivocally. This Method Collection will highlight state-of-the-art methods that have been explicitly designed to characterize glycans, glycoproteins, and glycopeptides derived from biological samples.