N-Glycan Modifications with Negative Charge in a Natural Polymer Mucin from Bovine Submaxillary Glands, and Their Structural Role
- Authors
- Kim, Jihye; Lee, Byoungju; Lee, Junmyoung; Ji, Minkyoo; Park, Chi Soo; Lee, Jaeryong; Kang, Minju; Kim, Jeongeun; Jin, Mijung; Kim, Ha Hyung
- Issue Date
- Jan-2021
- Publisher
- MDPI
- Keywords
- bovine submaxillary mucin; N-glycan; sulfate modification; structural role; functionality
- Citation
- POLYMERS, v.13, no.1
- Journal Title
- POLYMERS
- Volume
- 13
- Number
- 1
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/51989
- DOI
- 10.3390/polym13010103
- ISSN
- 2073-4360
2073-4360
- Abstract
- Bovine submaxillary mucin (BSM) is a natural polymer used in biomaterial applications for its viscoelasticity, lubricity, biocompatibility, and biodegradability. N-glycans are important for mucin stability and function, but their structures have not been fully characterized, unlike that of O-glycans. In this study, BSM N-glycans were investigated using liquid chromatography-tandem mass spectrometry. The microheterogeneous structures of 32 N-glycans were identified, and the quantities (%) of each N-glycan relative to total N-glycans (100%) were obtained. The terminal N-acetylgalactosamines in 12 N-glycans (sum of relative quantities; 27.9%) were modified with mono- (10 glycans) and disulfations (2 glycans). Total concentration of all sulfated N-glycans was 6.1 pmol in BSM (20 mu g), corresponding to 25.3% of all negatively charged glycans (sum of present N-glycans and reported O-glycans). No N-glycans with sialylated or phosphorylated forms were identified, and sulfate modification ions were the only negative charges in BSM N-glycans. Mucin structures, including sulfated N-glycans located in the hydrophobic terminal regions, were indicated. This is the first study to identify the structures and quantities of 12 sulfated N-glycans in natural mucins. These sulfations play important structural roles in hydration, viscoelasticity control, protection from bacterial sialidases, and polymer stabilization to support the functionality of BSM via electrostatic interactions.
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Collections - College of Pharmacy > School of Pharmacy > 1. Journal Articles
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