Wavelength tunability in photoinitiated cationic polymerization
Onium salts, widely used cationic photoinitiators, have absorption in the short wavelength of the UV spectrum. However, their spectral sensitivity can be tuned up to the visible region by using several methods. Photosensitization of onium salts, their charge transfer complex formation and their free radical promotion are some techniques that are used to provide wavelength flexibility. This chapter summarizes these methods. Upon irradiation photosensitizers such as anthracene, perylene and phenothiazine form exciplexes with onium salts generating reactive species via electron transfer. Furthermore, ground state charge transfer formation Correspondence/Reprint request: Dr. Y. Yagci, Istanbul Technical University, Department of Chemistry, Maslak, Istanbul 34469, Turkey. E-mail: yusuf@itu.edu.tr
Recent Developments of Versatile Photoinitiating Systems for Cationic Ring Opening Polymerization Operating at Any Wavelengths and under Low Light Intensity Sources
Photoinitiators (PI) or photoinitiating systems (PIS) usable in light induced cationic polymerization (CP) and free radical promoted cationic polymerization (FRPCP) reactions (more specifically for cationic ring opening polymerization (ROP)) together with the involved mechanisms are briefly reviewed. The recent developments of novel two- and three-component PISs for CP and FRPCP upon exposure to low intensity blue to red lights is emphasized in details. Examples of such reactions under various experimental conditions are provided.
Molecular diversity of skin mucus lectins in fish.
Among lectins in the skin mucus of fish, primary structures of four different types of lectin have been determined. Congerin from the conger eel Conger myriaster and AJL-1 from the Japanese eel Anguilla japonica were identified as galectin, characterized by its specific binding to beta-galactoside. Eel has additionally a unique lectin, AJL-2, which has a highly conserved sequence of C-type lectins but displays Ca(2+)-independent activity. This is rational because the lectin exerts its function on the cutaneous surface, which is exposed to a Ca(2+) scarce environment when the eel is in fresh water. The third type lectin is pufflectin, a mannose specific lectin in the skin mucus of pufferfish Takifugu rubripes. This lectin showed no sequence similarity with any known animal lectins but, surprisingly, shares sequence homology with mannose-binding lectins of monocotyledonous plants. The fourth lectin was found in the ponyfish Leiognathus nuchalis and exhibits homology with rhamnose-binding lectins known in eggs of some fish species. These lectins, except ponyfish lectin, showed agglutination of certain bacteria. In addition, pufflectin was found to bind to a parasitic trematode, Heterobothrium okamotoi. Taken together, these results demonstrate that skin mucus lectins in fish have wide molecular diversity.