Abstract
Nanoparticle receptors were synthesized through micellar imprinting to bind glycosphingolipids with 20-140 μM binding affinities, meanwhile distinguishing glycan composition, the number of acyl chains, and hydroxylation of acyl chains in the lipids. The strong binding enabled the receptors to protect their target glycolipids dispersed in lipid membranes from enzymatic degradation.
Highlights
Nanoparticle receptors were synthesized through micellar imprinting to bind glycosphingolipids with 20–140 lM binding affinities, distinguishing glycan composition, the number of acyl chains, and hydroxylation of acyl chains in the lipids
The strong binding enabled the receptors to protect their target glycolipids dispersed in lipid membranes from enzymatic degradation
Scheme 1 shows the preparation of molecularly imprinted nanoparticle (MINP) receptors for these lipids
Summary
In addition to promoting membrane packing and raft formation, they play important roles in cell signaling and regulation.[1] Their metabolites, including sphingosine and lysosphingolipids, have a plethora of biological functions including the regulation of cell growth, survival, immune cell trafficking, and development of inflammation and cancer.[2,3,4] synthetic receptors for these molecules could have many potential applications,[5,6,7,8,9] selective recognition of glycosphingolipids (and carbohydrates in general) has been difficult because of the strong solvation of glycans in water and the subtle difference of their structures, often by the stereochemistry of a single hydroxyl. Their sizes (4–5 nm) were determined by DLS and had been confirmed by TEM.[21,22] Their bindings with 1–5 were determined by isothermal titration calorimetry (ITC) and
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
