Because of the pressing needs to comprehensively understand the biological attributes of glycosylation in many important biological functions such as the immune response, cell development, cellular differentiation/adhesion and host-pathogen interactions, glycomics and glycoproteomics continue to be highly dynamic and interesting research areas. Moreover, aberrant glycosylation for decades has been recognized as the attribute of many mammalian diseases, including osteoarthritis, cystic fibrosis and cancer. The diverse biological roles of glycans and their implications in diseases have created a demand for reliable quantitative glycomic approaches, permitting sensitive monitoring of glycans in biological systems.
The aim of this proposal is the creation of glycomic mapping platform enabling the automated identification, annotation and quantitation of glycans derived from biological samples. The platform comprises of both analytical methods and bioinformatic tools. The analytical methods are based on reversed-phase liquid chromatography and mass spectrometry of permethylated glycans while the bioinformatic tools facilitate automation of interpretation and quantitation. The glycomic mapping platform will be employed to understand the biological attributes of glycan in disease development, such as cancer and cardiovascular diseases.
The proposed research activities are aimed at the creation of analytical methods and bioinformatic tools to facilitate rapid and detailed characterization of glycoproteins. Such effort is aimed at facilitating better understanding of the biological roles of glycosylation. The resulting methods and tools will create a glycomic mapping platform that will allow sensitive, reliable and reproducible monitoring of alteration in glycosylation as a result of perturbation in biological systems such as changes in glycosylation as a result of disease progression.
|Banazadeh, Alireza; Veillon, Lucas; Wooding, Kerry M et al. (2016) Recent advances in mass spectrometric analysis of glycoproteins. Electrophoresis :|
|Yin, Haidi; Zhu, Jianhui; Wu, Jing et al. (2016) A procedure for the analysis of site-specific and structure-specific fucosylation in alpha-1-antitrypsin. Electrophoresis 37:2624-2632|
|Abou-Abbass, Hussein; Abou-El-Hassan, Hadi; Bahmad, Hisham et al. (2016) Glycosylation and other PTMs alterations in neurodegenerative diseases: Current status and future role in neurotrauma. Electrophoresis 37:1549-61|
|Abou-Abbass, Hussein; Bahmad, Hisham; Abou-El-Hassan, Hadi et al. (2016) Deciphering glycomics and neuroproteomic alterations in experimental traumatic brain injury: Comparative analysis of aspirin and clopidogrel treatment. Electrophoresis 37:1562-76|
|Elmasri, Wael A; Yang, Tianjiao; Hegazy, Mohamed-Elamir F et al. (2016) Iridoid glycoside permethylation enhances chromatographic separation and chemical ionization. Rapid Commun Mass Spectrom 30:2033-42|
|Wooding, Kerry M; Peng, Wenjing; Mechref, Yehia (2016) Characterization of Pharmaceutical IgG and Biosimilars Using Miniaturized Platforms and LC-MS/MS. Curr Pharm Biotechnol 17:788-801|
|Zhou, Shiyue; Hu, Yunli; Mechref, Yehia (2016) High-temperature LC-MS/MS of permethylated glycans derived from glycoproteins. Electrophoresis 37:1506-13|
|Dong, Xue; Zhou, Shiyue; Mechref, Yehia (2016) LC-MS/MS analysis of permethylated free oligosaccharides and N-glycans derived from human, bovine, and goat milk samples. Electrophoresis 37:1532-48|
|Zhao, Jingfu; Song, Ehwang; Zhu, Rui et al. (2016) Parallel data acquisition of in-source fragmented glycopeptides to sequence the glycosylation sites of proteins. Electrophoresis 37:1420-30|
|Zhou, Shiyue; Tello, Nadia; Harvey, Alex et al. (2016) Reliable LC-MS quantitative glycomics using iGlycoMab stable isotope labeled glycans as internal standards. Electrophoresis 37:1489-97|
Showing the most recent 10 out of 22 publications