Prenyl sulfates as alkylating reagents for mercapto amino acids.

A new methodology for prenylation of thiol compounds has been developed. The approach is based on the use of prenyl sulfates as new reagents for S-prenylation of benzenethiol and cysteamine in aqueous systems. The C(10)-prenols geraniol and nerol that differ in the configuration (E or Z, correspondingly) of the alpha-isoprene unit were efficiently O-sulfated in the presence of a pyridine-SO(3') complex. The obtained geranyl and neryl sulfates were tested as alkylating agents. These compounds were chosen to reveal the influence of the alpha-isoprene unit configuration on their alkylation (prenylation) ability. S-Geranyl cysteine was prepared to demonstrate the applicability of this method for prenylation of peptides containing mercapto amino acids.

Chemical synthesis of dolichyl phosphates, their analogues and derivatives and application of these compounds in biochemical assays.

Several methods for simple and efficient chemical synthesis of dolichyl phosphates and their analogues and derivatives are briefly summarized with a special emphasis on chemical modification of phosphoryl group and preparation of dolichyl phosphates labelled at the omega-end and at the gamma-isoprene unit of the isoprene chain by fluorescent groups, 2-aminopyridine and 1-aminonaphtalene residues. Additionally, data on biochemical assays with application of the compounds mentioned above are presented.

Synthesis of a quaternary polyprenyl ammonium salt.

Reaction of primary C(55)-allylic alcohol moraprenol (WT(3)C(7-9)-OH, a polyprenol from mulberry leaves) with triethylamine in the presence of phosphorus oxychloride leads to a quaternary ammonium chloride with a good yield (72%) and high cis-stereoselectivity of the terminal isoprene unit. Cationic polyprenyl derivatives may be useful for transfection and immunological studies.

Diversity in isoprene unit biosynthesis: The methylerythritol phosphate pathway in bacteria and plastids

The long-overlooked methylerythritol phosphate (MEP) pathway represents an alternative to the mevalonate route for the formation of isoprene units. It is found in most bacteria as well as in the plastids of all phototrophic organisms. A selection of significant steps of its discovery and elucidation are presented in this contribution, as well as a complete hypothetical biogenetic scheme for the last reduction step.