Dataset Advancement: Glycan Composition and Peptide Mass Fingerprinting of the Native Torpedo californica Nicotinic Acetylcholine Receptor after a Multi-Step Sequential Purification Method

The study described in this dataset focuses on the characterization of the nicotinic acetylcholine receptor (nAChR), a member of the Cys-loop pentameric ligand-gated ion channels that play critical roles in organismal function. Our research efforts have resulted in the successful production of a highly pure nAChR, which has allowed for more robust studies to be conducted, including high-throughput crystallization experiments. Using advanced technologies such as Nano Lc MS/MS and MALDI ToF/ToF, we have identified and extensively characterized each nAChR subunit, achieving a 100% identity. Furthermore, we have investigated the N-linked glycans in the Torpedo californica-nAChR (Tc-nAChR) subunits. By digesting the Tc-nAChR subunits with PNGase F and analyzing the released glycans with MALDI-ToF, we identified the presence of high-mannose N-glycan in all native Tc-nAChR subunits. Specifically, we observed the oligommanose population Man8-9GlcNac2 with peaks at m/z 1742 and 1904 ([M + Na]+ ions). Overall, this study emphasizes the importance of continued research efforts aimed at understanding the complex biology of the Cys-loop pentameric ligand-gated ion channels and their involvement in organismal function and disease. The insights gained from such studies could have far-reaching implications for the development of new therapeutic strategies to combat a wide range of health issues.