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Jinshan Gao

Associate Professor, Chemistry and Biochemistry

Office:
Richardson Hall 344
Email:
gaoj@montclair.edu
Phone:
973-655-5136
Degrees:
BS, China Agricultural University
PhD, Purdue University
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Profile

My research interests lie in 1) the development of free radical reagents for glycan and protein structure elucidation, 2) the identification and discovery of potential serum biomarkers for cancers, and 3) study of the molecular mechanism of these diseases by combining biomimetic reagents and high-throughput mass spectrometry. We recently developed methylated free radical activated glycan sequencing reagent (Me-FRAGS) which significantly simplify the systematic analysis of complex glycan structures using mass spectrometry (http://pubs.rsc.org/en/content/articlelanding/2016/sc/c6sc01371f). This approach provides valuable information for glycan structure analysis and offers unique advantages compared to earlier studies. In order to apply this approach to the identification of potential glycan biomarkers for cancers, resin-supported and magnetic nanoparticle-based free radical reagent are being designed and synthesized.

Bioinformatics tools for the analysis of DNA (RNA) and protein sequences have been well developed. However, these tools cannot be directly applied to glycan bioinformatics due to the fact that glycan can exhibit complicated branch structures. As with proteomics, mass spectrometry (MS) has been broadly utilized for the characterization of glycans. Unfortunately, no efficient software tools were available to interpret the spectra due to the complexity of glycan structure. Recently, our group has developed free radical reagents for glycan structure characterization. These free radical reagents exhibit high fragmentation efficiency and systematic fragmentation. However, the interpretation of spectra has to be done manually. In order to overcome this barrier, we developed a glycan fragmentation assignment software denominated as “Glyc”. Here is a link to Glyc: http://www.ericjoycefilm.com/client/glyc
Here is a link to the video tutorial: http://www.ericjoycefilm.com/reel/_2015/glyc


Currently, we are looking for lab specialist with a strong background of mass spectrometry and organic synthesis. If you are interested in this position, send email to gaoj@montclair.edu.

Specialization

Proteomics and glycomics by employing free radical chemistry and mass spectrometry

Resume/CV

Office Hours

Fall

Tuesday
8:30 am - 9:30 am
Thursday
8:30 am - 9:30 am
Friday
8:30 am - 9:30 am

Links

Research Projects

Biomimetic reagents for protein, glycan, and glycoprotein structural analysis

Mass spectrometric glycan rearrangement is problematic because it provides misleading structural information. Collisional activation of Me-FRAGS-derivatized glycans generates a nascent free radical that concurrently induces abundant glycosidic bond and cross-ring cleavages without the need for subsequent activation. Product ions resulting from glycan rearrangement, including internal residue loss and multiple external residue losses, are precluded. Glycan structures can be easily assembled and visualized via a radical driven glycan deconstruction diagram (R-DECON diagram). The presence and locations of N-acetylated saccharide units and branch sites can be identified by the characteristic dissociation patterns observed only at these locations. Mechanisms of dissociation are investigated and discussed. This Me-FRAGS based mass spectrometric approach creates a new blueprint for glycan structure analysis.

Development of software for interpretation of glycan spectra induced by free radical

Bioinformatics tools for the analysis of DNA (RNA) and protein sequences have been well developed. However, these tools cannot be directly applied to glycan bioinformatics due to the fact that glycan can exhibit complicated branch structures. As with proteomics, mass spectrometry (MS) has been broadly utilized for the characterization of glycans. Unfortunately, no efficient software tools were available to interpret the spectra due to the complexity of glycan structure. Recently, our group has developed free radical reagents for glycan structure characterization. These free radical reagents exhibit high fragmentation efficiency and systematic fragmentation. However, the interpretation of spectra has to be done manually. In order to overcome this barrier, we aim to develop a glycan fragmentation assignment software denominated as “Glyc”.

Development of Multiple-Functional Free Radical Reagent for Glycoprotein/Glycan Characterization and Enrichment

Glycoproteins are ubiquitous components of extracellular matrices and cellular surfaces, and have been reported to have unique structural and functional roles in cell-cell, cell-matrix recognition, protein stability, protein localization, and immune response. Over 50% of human proteins are estimated to be potentially glycosylated. Hence, there is considerable interest to develop strategies aiming at full characterization of glycosylation in proteins, particularly in complex biological mixtures. Glycan moiety, which is covalently attached to specific amino acids (glycosylation sites) of protein, generally has complex structures due to the structural intricacies and diversity. Alterations of glycan expression in glycoprotein have been associated with many diseases, such as cancers, diabetes, inflammatory diseases, rheumatoid arthritis, Alzheimer’s diseases, Pompe diseases, and immune disorders. Meanwhile, the identification of glycosylation site is also crucial for deciphering physiological relevance and potential value as a diagnostic. Therefore profiling the disease-associated glycoproteins is essential for the understanding of their functions at a molecular level, and thus benefits the identification of diagnostic glycoprotein and/or glycan biomarkers and the better design of therapeutic drugs.

We aim to develop solid-supported free radical probes (SSFRP) for glycan enrichment and characterization, and free radial activated glycoprotein structure elucidation (FRAGPSE) reagent for glycoprotein characterization. In ongoing experiments, we develop free radical reagents that significantly simplify the characterization of complex glycoprotein and glycan structures by taking advantage of free radical chemistry and collision-induced dissociation (CID: simple, reproducible, and mature dissociation technique). This allows glycan and glycoprotein characterization broadly accessible and cost-effective for the end-user.

Biomarkers discovery for early disease detection

We are seeking potential collaboration for the application of the novel free radical technique to discover potential glycan, protein, glycoprotein biomarkers for early detection of disease, such as cancer.