105943-89-3Relevant academic research and scientific papers
Fluorinated Pseudopeptide Analogues of the Neuropeptide 26RFa: Synthesis, Biological, and Structural Studies
Pierry, Camille,Couve-Bonnaire, Samuel,Guilhaudis, Laure,Neveu, Cindy,Marotte, Amelie,Lefranc, Benjamin,Cahard, Dominique,Segalas-Milazzo, Isabelle,Leprince, Jerome,Pannecoucke, Xavier
, p. 1620 - 1633 (2013)
A series of four fluorinated dipeptide analogues each containing a fluoro-olefin moiety as peptide bond surrogate has been designed and synthesized. These motifs have been successfully introduced into the bioactive C-terminal heptapeptide of the neuropeptide 26RFa by conventional SPPS. We then evaluated the ability of the generated pseudopeptides to increase [Ca2+]i in GPR103-transfected cells. For these fluorinated analogues, greater stability in human serum was observed. Their conformations were also investigated, leading to the valuable identification of differences depending on the position of the fluoro-olefin moiety in the sequence.
Synthetic and Enzyme Inhibition Studies of Pepstatin Analogues Containing Hydroxyethylene and ketomethylene Dipeptide Isosteres
Holladay, Mark W.,Salituro, Francesco G.,Rich, Daniel H.
, p. 375 - 383 (2007/10/02)
Synthetic details for the preparation of a series of hydroxyethylene and ketomethylene dipeptide isosteres with control of stereochemistry at C(2) are described.Incorporation of the isosteres into peptide sequences derived from pepstatin afforded potent inhibitors of the aspartic protease porcine pepsin.When or was substituted with statine ((3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid), inhibitors equipotent to the parent compound were obtained, whereas was a much less effective replacement for statine.A similar trend was evident in the corresponding ketones.The finding that structural features for good substrates do not closely parallel those for good inhibitors is discussed.
