A Novel Synthetic Route For The Preparation Of Ammonium And Alkali-Metal Tetrafluoroborates And Alkyl Substituted Ammonium Tetrafluoroborates Using Pyridinium Tetrafluoroborate As The Precursor

Ammonium and alkali metal tetrafluoroborates have been prepared by the cation exchange reaction of pyridinium tetrafluoroborate with the corresponding hydroxides/halides. The reaction of pyridinium tetrafluoroborate with primary, secondary and tertiary alkyl amines at room temperature gives rise to mono-, di- and tri-alkylammonium tetrafluoroborates, respectively. The yields are good and the samples are of high purity. The products have been characterised by elemental analysis, IR and PMR spectroscopy. The spectral data for most of the compounds are reported for the first time.

REACTION OF THIOPHOSPHORYL FLUORIDE AND THIOPHOSPHORYL CHLORIDE WITH DIMETHYL SULPHOXIDE

Solid complexes of thiophosphoryl fluoride and thiophosphoryl chloride with dimethyl sulphoxide (DMSO) have been prepared and characterized.

Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins

The critical, and often most difficult, step in structure elucidation of diverse classes of natural peptides is the determination of correct disulfide pairing between multiple cysteine residues. Here, we present a direct mass spectrometric analytical methodology for the determination of disulfide pairing. Protonated peptides, having multiple disulfide bonds, fragmented under collision induced dissociation (CID) conditions and preferentially cleave along the peptide backbone, with occasional disulfide fragmentation either by C-beta-S bond cleavage through H-alpha abstraction to yield dehydroalanine and cysteinepersulfide, or by S-S bond cleavage through H-beta abstraction to yield the thioaldehyde and cysteine. Further fragmentation of the initial set of product ions (MSn) yields third and fourth generation fragment ions, permitting a distinction between the various possible disulfide bonded structures. This approach is illustrated by establishing cysteine pairing patterns in five conotoxins containing two disulfide bonds. The methodology is extended to the Conus araneosus peptides An 446 and Ar1430, two 14 residue sequences containing 3 disulfide bonds. A distinction between 15 possible disulfide pairing schemes becomes possible using direct mass spectral fragmentation of the native peptides together with fragmentation of enzymatically nicked peptides.