The unique properties of dipeptidyl-peptidase IV (DPP IV / CD26) and the therapeutic potential of DPP IV inhibitors.

This review deals with the properties and functions of dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5). This membrane anchored ecto-protease has been identified as the leukocyte antigen CD26. The following aspects of DPP IV/CD26 will be discussed : the structure of DPP IV and the new family of serine proteases to which it belongs, the substrate specificity, the distribution in the human body, specific DPP IV inhibitors and the role of CD26 in the intestinal and renal handling of proline containing peptides, in cell adhesion, in peptide metabolism, in the immune system and in HIV infection. Especially the latest developments in the search for new inhibitors will be reported as well as the discovery of new natural substrates for DPP IV such as the glucagon-like peptides and the chemokines. Finally the therapeutical perspectives for DPP IV inhibitors will be discussed.

Influence of N substitution on antimycobacterial activity of ciprofloxacin.

Ciprofloxacin analogs with various substitutions on the piperazine nitrogen were tested against several mycobacteria. In contrast to what has been found with other gram-positive and gram-negative bacteria, alkyl analogs such as N-isopropylciprofloxacin were shown to be significantly more active than ciprofloxacin. MICs of 0.125 microgram/ml against Mycobacterium tuberculosis were found.

The mycobacterial cell-wall as target for antimycobacterial drugs. I--Synthesis and activity of some diphenylalkylanalogues of mycolic acids.

Mycolic acids are 2-alkyl-3-hydroxyfatty acids and are essential parts of the peptidoglycan of mycobacteria. Potential antimetabolites were prepared by substituting a longchain alkylgroup by a diphenylmethylfunction. 3-Oxo esters and 3-hydroxy esters and acids were prepared. The 3-oxo esters showed a slight activity against M. tuberculosis and some atypical mycobacteria.