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Abstract
The first single‐molecule fluorescence detection of a structurally‐defined synthetic carbohydrate is reported: a heparan sulfate (HS) disaccharide fragment labeled with Alexa488. Single molecules have been measured whilst freely diffusing in solution and controlled encapsulation in surface‐tethered lipid vesicles has allowed extended observations of carbohydrate molecules down to the single‐molecule level. The diverse and dynamic nature of HS–protein interactions means that new tools to investigate pure HS fragments at the molecular level would significantly enhance our understanding of HS. This work is a proof‐of‐principle demonstration of the feasibility of single‐molecule studies of synthetic carbohydrates which offers a new approach to the study of pure glycosaminoglycan (GAG) fragments.
Highlights
Single-molecule fluorescence spectroscopy has revolutionized the study of biological molecules.[1]
While carbohydrates have been modified with fluorescent dyes for ensemble studies,[2,3] this does not guarantee the homogeneity and photostability required for single-molecule detection
Owing to the similarity between the protein-binding regions (NS domains) of heparan sulfate (HS) and the related GAG heparin, the major glucosamine-iduronic acid heparin disaccharide is a useful model of HS and was chosen for fluorescent labeling
Summary
Single-molecule fluorescence spectroscopy has revolutionized the study of biological molecules.[1]. Single-molecule fluorescence spectroscopy has revolutionized the study of biological molecules.[1] In contrast to nucleic acids and proteins, for which single-molecule detection has been well exploited, applications to structurally-defined carbohydrates have not yet been reported, in part owing to the requirement for non-trivial synthetic chemistry.
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