The importance of the hydrogen bonding interactions in the GLUT-hexose bindingp rocess (GLUT = hexose transporter) has been demonstrated by studying the binding of structurally modified d-fructose analoguest oG LUTs, and in one case its transport into cells. The presence of ah ydrogen bond donor at the C-3 positiono f2 ,5-anhydro-d-mannitol derivatives is essential for effective bindingt oG LUT5 and transport into tumor cells. Surprisingly,i nstallation of ag roup that can function only as ah ydrogen bond acceptor at C-3 resulted in selective recognition by GLUT1 rather than GLUT5.Afluorescently labelled analoguec learly showed GLUT-mediated transport and low efflux properties of the probe.T his study reveals that as ingle positional modification of a2 ,5-anhydro-d-mannitol derivativei ssufficient to switch its binding preferencef rom GLUT5 to GLUT1,a nd uncovers general scaffolds that are suitable for the potential selectived elivery of molecular payloads into tumorc ells via GLUT transport machinery.

An efficient and facile protocol to functionalize position C-3 of 2,5-anhydro-D-mannitol via diastereoselective ring opening of a C 2 -symmetric epoxide 2,5:3,4-dianhydro-D-allitol 3 has been developed. This method is protecting-group-free, high-yielding, and provides access to C-3-modified 2,5-anhydro-D-mannitols 5a, 11a-15a and 16-17. This method was then extrapolated to the synthesis of a C 2 -symmetric aziridine, which underwent ring opening with various nucleophiles to provide

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