大澤 重仁
Department Research Institutes and Facilities, Research Institutes and Facilities Position |
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Article types | Original article |
Language | English |
Peer review | Peer reviewed |
Title | Direct Observation of Cell Surface Sialylation by Atomic Force Microscopy Employing Boronic Acid–Sialic Acid Reversible Interaction |
Journal | Formal name:Analytical chemistry Abbreviation:Anal Chem ISSN code:00032700/15206882 |
Domestic / Foregin | Foregin |
Volume, Issue, Page | 92(17),pp.11714-11720 |
Author and coauthor | Shigehito Osawa, Akira Matsumoto, Yukie Maejima, Toshihiro Suzuki, Yuji Miyahara, Hidenori Otsuka |
Authorship | Lead author |
Publication date | 2020/07/29 |
Summary | Tracing cell surface sialylation dynamics at a scale of the glycolipoprotein microdomain (lipid rafts) formations remains an intriguing challenge of cellular biology. Here, we demonstrate that this goal is accessible, taking advantage of a boronic acid (BA)-based reversible molecular recognition chemistry. A BA-end-functionalized poly(ethylene glycol) was decorated onto an atomic force microscopy (AFM) cantilever, which provided a dynamic and sialic acid (SA)-specific imaging mode. Using this technique, we were able to heat map the SA expression levels not only on protein-decorated substrates but also directly on the cell surfaces, with a submicrometer scale resolution that may be relevant to that of the lipid rafts formation. The SA specificity and the binding reversibility of the probe were confirmed from its pH-dependent characteristics and an inhibition assay using free state SA. This finding may provide a noninvasive means for assessing a variety of SA-involved glycosylation dynamics spanning from physiology to pathology. |
DOI | https://doi.org/10.1021/acs.analchem.0c01705 |