172834-25-2Relevant academic research and scientific papers
Fluoro-olefins as peptidomimetic inhibitors of dipeptidyl peptidases
Van Der Veken, Pieter,Senten, Kristel,Kertèsz, István,De Meester, Ingrid,Lambeir, Anne-Marie,Maes, Marie-Berthe,Scharpé, Simon,Haemers, Achiel,Augustyns, Koen
, p. 1768 - 1780 (2007/10/03)
The feasibility of the fluoro-olefin function as a peptidomimetic group in inhibitors for dipeptidyl peptidase IV and II (DPP IV and DPP II) is investigated by evaluation of N-substituted Gly-Ψ[CF=C]pyrrolidines, Gly-Ψ[CF=C]piperidines, and Gly-Ψ[CF=C](2-cyano)pyrrolidines. Of this later class, the (Z)- and (E)-fluoro-olefin analogues were prepared and chemical stability in comparison with the parent amide was checked. Most of these compounds exhibited a strong binding preference toward DPP II with IC 50 values in the low micromolar range, while only low DPP IV inhibitory potential is seen.
Bradykinin receptor antagonists containing N-substituted amino acids: In vitro and in vivo B2 and B1 receptor antagonist activity
Goodfellow, Val S.,Marathe, Manoj V.,Kuhlman, Karen G.,Fitzpatrick, Timothy D.,Cuadrado, David,Hanson, Wendy,Zuzack, John S.,Ross, Sherman E.,Wieczorek, Maciej,Burkard, Michael,Whalley, Eric T.
, p. 1472 - 1484 (2007/10/03)
We report a systematic probing of the structural requirements of the bradykinin (BK) type 2 (B2) receptor for antagonist activity by incorporating N-alkyl-amino acid residues at positions 7 and 8 of a potent antagonist sequence. Compound 1 (D-A
