192821-72-0Relevant academic research and scientific papers
Pyrrolidides: synthesis and structure-activity relationship as inhibitors of dipeptidyl peptidase IV
Augustyns, K. J. L.,Lambeir, A. M.,Borloo, M.,Nmeester, I. De,Vedernikova, I.,et al.
, p. 300 - 310 (2007/10/03)
Dipeptidyl peptidase IV cleaves specifically the peptide bond at the carbonyl side of a proteine at the penultimate N-terminal position of a peptide.It is shown to be important for the regulation of biologically active peptides.Moreover, It has been identified as an activation marker of T-lymphocytes (CD26).Pyrrolidides and thiazolidides are known as reversible inhibitors of DPP IV.Several homologues, unsaturated, open and 3-substituted analogues were synthesized in order to determine the structure-activity relationship of the P-1 site.L-Isoleucine was taken as P-2amino acid. 1-(L-Isoleucyl)-3(S)-fluoropyrrolidine is about as active as the non-fluorinated compound and behaves as competitive inhibitor.Other changes decrease or abolish the activity. - Keywords: dipeptidyl peptidase IV/ pyrrolidine/ serine protease/ proline peptidase/ protease inhibitor.
