5978-88-1Relevant articles and documents
(Trifluoromethylselenyl)methylchalcogenyl as Emerging Fluorinated Groups: Synthesis under Photoredox Catalysis and Determination of the Lipophilicity
Grollier, Kevin,De Zordo-Banliat, Arnaud,Bourdreux, Flavien,Pegot, Bruce,Dagousset, Guillaume,Magnier, Emmanuel,Billard, Thierry
supporting information, p. 6028 - 6033 (2021/03/15)
The synthesis of molecules bearing (trifluoromethylselenyl)methylchalcogenyl groups is described via an efficient two-step strategy based on a metal-free photoredox catalyzed decarboxylative trifluoromethylselenolation with good yields up to 88 %, which raised to 98 % in flow chemistry conditions. The flow methods allowed also to scale up the reaction. The mechanism of this key reaction was studied. The physicochemical characterization of these emerging groups was performed by determining their Hansch–Leo lipophilicity parameters with high values up to 2.24. This reaction was also extended to perfluoroalkylselenolation with yields up to 95 %. Finally, this method was successfully applied to the functionalization of relevant bioactive molecules such as tocopherol or estrone derivatives.
A low-molecular-weight supramolecular hydrogel of riboflavin bolaamphiphile for VEGF-siRNA delivery
Patil, Sachin Prakash,Jeong, Hyun Seok,Kim, Byeang Hyean
supporting information, p. 8901 - 8903 (2012/11/14)
A low-molecular-weight hydrogel derived from riboflavin (vitamin B 2) that self-assembles to provide supramolecular nanofibers, biocompatible material, can be used to deliver VEGF-siRNA efficiently into human cells by the endocytosis pathway, where the siRNA is functionalized.
Dynamically modified, biospecific optical fiber sensor for riboflavin binding protein based on hydrophobically associated 3-octylriboflavin
Ogasawara, Faye K.,Wang, Yunlong,Bobbitt, Donald R.
, p. 1637 - 1642 (2007/10/02)
A new approach to the production of optical fiber sensors Is described which Is based on a dynamic modification procedure. In this approach, the optical fiber surface is rendered Hydrophobic through the covalent attachment of a C18 moiety. Specific sensing ligands are then associated with this surface through either their inherent or designed hydrophobicity. To investigate the feasibility of the approach, an optical fiber sensor has been constructed for riboflavin binding protein in which 3-octylriboflavin is associated with the fiber surface. Fluorescence quenching occurs upon binding of the protein to the immobilized riboflavin derivative. The sensor possesses a minimum measurable quantity of 7.3 pmol of binding protein in a probe volume which is less than 10 μL. With this approach, the sensing surface was repetitively regenerated 15 times over a 1-h period with less than a 5% variation in sensor-to-sensor performance. The approach is general, and with minor variations it can be used in a variety of sensing situations.