Explore the vast range of titles available.

Phase-transfer catalysis (PTC) is widely used in glycochemistry for the preparation of aryl glycosides by the glycosylation reaction. While investigating the possibility of synthesis of 4-(3-chloropropoxy)phenyl sialoside (Neu5Ac-OCPP) from N-acetylsialyl chloride with O-acetyl groups (1), we have recently discovered a strong dependence of the PTC glycosylation outcome on the mixing mode: under batch conditions, only α-anomer of Neu5Ac-OCPP was obtained, albeit in low yield (13%), while under microfluidic conditions the yield of Neu5Ac-OCPP increased to 36%, although stereoselectivity decreased (α/β ≤ 6.2). Here, we report that the outcome of this reaction, performed under microfluidic conditions using a Comet X-01 micromixer (at 2 μL/min flow rate), non-linearly depends on the concentration of N-acetylsialyl chloride 1 (5–200 mmol/L). The target Neu5Ac-OCPP was obtained in a noticeably higher yield (up to 66%) accompanied by enhanced stereoselectivity (α/β = 17:1–32:1) in the high concentration range (C > 50 mmol/L), whereas the yield (10–36%) and especially, stereoselectivity (α/β = 0.9:1–6.2:1) were lower in the low concentration range (C ≤ 50 mmol/L). This dramatic stepwise increase in stereoselectivity above critical concentration (50 mmol/L) is apparently related to the changes in the presentation of molecules on the surface of supramers of glycosyl donor, which exist in different concentration ranges.

Flow chemistry offers several advantages for performing chemical reactions and has become an important area of research. It may seem that sufficient knowledge has already been acquired on this topic to understand how to choose the design of microreactor/micromixer and flow rate in order to achieve the desired outcome of a reaction. However, some experimental data are difficult to explain based on commonly accepted concepts of chemical reactivity and performance of microfluidic systems. In this mini review, we attempt to identify such data and offer a rational explanation of unusual results based on the supramer approach. We demonstrate that variation in flow regime (determined by mixer design and flow rate) can either improve or worsen the reactivity and lead to completely different products, including stereoisomers. It is not necessary to mix the reagents with maximum efficiency. The real challenge is to mix reagents the right way since at a too high or too low flow rate (in the particular mixer), the molecules of reagents are incorrectly presented on the surface of supramers, leading to altered stereoselectivity, or form tight supramers, in which most of the molecules are located inside the supramer core and are inaccessible for attack, leading to low yields.

The synthetic function‐spacer‐lipid (FSL) amphiphile biotin‐CMG‐DOPE is widely used for delicate ligation of living cells with biotin residues under physiological conditions. Since this molecule has an “apolar‐polar‐hydrophobic” gemini structure, the supramolecular organization is expected to differ significantly from the classical micelle. Its organization is investigated with experimental methods and molecular dynamics simulations (MDS). Although the linear length of a single biotin‐CMG‐DOPE molecule is 9.5 nm, the size of the dominant supramer globule is only 14.6 nm. Investigations found that while the DOPE tails form a hydrophobic core, the polar CMG spacer folds back upon itself and predominantly places the biotin reside inside the globule or planar layer. MDS demonstrates that <10 % of biotin residues on the highly water dispersible globules and only 1 % of biotin residues in layer coatings are in an linear conformation and exposing biotin into the aqueous medium. This explains why in biotin‐CMG‐DOPE apolar biotin residues both in water dispersible globules and coatings on solid surfaces are still capable of interacting with streptavidin. Binding cells together: Gemini amphiphile biotin‐CMG‐DOPE when coated on a surface forms a monolayer where quite non‐polar biotin residues are hidden in the hydrophobic DOPE zone, however ∼1 % of biotins are able to dynamically pop‐up and, therefore, bind to streptavidin.