Synthesis and triplex forming ability of conformationally locked oligonucleotides containing unnatural nucleobases: efficient recognition of a C.G interruption.

In order to develop a novel nucleoside analogue which recognizes C.G interruption in homopurine.homopyrimidine DNA, we designed and synthesized a conformationally locked nucleoside analogue, 1-(2-O,4-C-methylene-beta-D-ribofuranosyl)pyridin-2-one (4), and introduced it into a triplex-forming oligonucleotide (TFO). On melting temperature (Tm) measurements, the unprecedented C.G base recognition ability of 4 was observed.     

Identification of fibronectin fragments that bind to carboxy-group-modified proteins.

Limited proteolysis of human plasma fibronectin with chymotrypsin, trypsin or thermolysin has been used to localize binding sites responsible for binding [Vuento, Korkolainen & Stenman (1982) Biochem. J. 205, 303-311] of fibronectin to carboxy-group-modified proteins. These bindings sites are different from those mediating binding of fibronectin to gelatin or heparin. They are located close to the C-terminus of the polypeptide chains of fibronectin, and apparently overlap with the C-terminal fibrin binding site.