Matthew H. Lyttle

Solid Phase Synthesis of Dual Labeled Peptides: Development of Cell Permeable Calpain Specific Substrates

A step-by-step evaluation of dual-labeled FRET substrates for the protease calpain is reported. The study led to cell permeable selections, with optimized specificity and effectiveness for the target enzyme, and improved stability to non-specific degrading enzymes.

Chain cleavage during deprotection of RNA synthesized by the 2'-O-trialkylsilyl protection strategy

Abstract The side reaction of inter-ribonucleotide bond cleavage occuring during ammonia treatment for deprotection of support bound 2′-O-trialkylsilyl protected synthetic RNA has been assessed by analysis of a series of 15 mers of sequence T4XT10 where x is rA, rC, rG and U. Data derived from HPLC analysis of the products showed, in all cases, cleavage by the anhydrous ammonia to be dramatically reduced compared to that with ethanolic concentrated aqueous ammonia. The anhydrous reagent also gave improved product quality when used in the synthesis of a 50 residue sequence. Complete cleavage of exocyclic amine protection groups with the anhydrous reagent was confirmed by RNAse T2 digests.