ABSTRACT Given the prominence of 19 F‐bioNMR in structural research, fluorinated glycan frameshifts hold enormous potential in studying carbohydrate‐protein interactions. To contribute to this field, the synthesis of selectively C‐2 fluorinated glycans related to the O3b antigen of Klebsiella pneumoniae is disclosed, and their interactions with the lectin Concanavalin A (ConA) are interrogated spectroscopically. Automated glycan assembly (AGA) was employed to expedite construction in which the C(sp 3 )‐F bond was leveraged to control stereoselectivity of α‐mannosylation. Subsequent 19 F‐BioNMR analysis of binding to ConA allowed determination of the respective IC 50 and K D values; this revealed a conspicuous frameshift‐dependency in which one pattern dominated. Collectively, this study advocates for the strategic utilisation of the C(sp 3 )‐F bond in the design, construction, and analysis of probes to interrogate ubiquitous mannose‐binding lectins with therapeutic relevance.
Suri et al. (2026) studied this question.