ulodesine and galidesivir

ulodesine has been researched along with galidesivir* in 1 studies

Other Studies

1 other study(ies) available for ulodesine and galidesivir

Article	Year
Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase. Journal of medicinal chemistry, 2009, Feb-26, Volume: 52, Issue:4 ImmH (1) and DADMe-ImmH (2) are potent inhibitors of human purine nucleoside phoshorylase (PNP), developed by us and currently in clinical trials for the treatment of a variety of T-cell related diseases. Compounds 1 and 2 were used as templates for the design and synthesis of a series of acyclic immucillin analogues (8-38) in order to identify simplified alternatives to 1 and 2. SerMe-ImmG (8) and DATMe-ImmG (9) displayed the lowest inhibition constants of 2.1 and 3.4 pM, respectively, vs PNP. It was postulated that the flexible natures of 8 and 9 enabled them to adopt conformations resembling those of 1 and 2 within the active site of PNP and that the positioning of two hydroxyl groups was critical for picomolar activity. SerMe-ImmH (10, K(d) = 5.2 pM) was shown to be orally available in mice with a long biological residence time on blood PNP. Topics: Adenine; Adenosine; Catalytic Domain; Drug Design; Humans; Molecular Conformation; Pliability; Protein Binding; Purine-Nucleoside Phosphorylase; Pyrrolidines; Structure-Activity Relationship	2009

Article

Year

Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase.

Journal of medicinal chemistry, 2009, Feb-26, Volume: 52, Issue:4

ImmH (1) and DADMe-ImmH (2) are potent inhibitors of human purine nucleoside phoshorylase (PNP), developed by us and currently in clinical trials for the treatment of a variety of T-cell related diseases. Compounds 1 and 2 were used as templates for the design and synthesis of a series of acyclic immucillin analogues (8-38) in order to identify simplified alternatives to 1 and 2. SerMe-ImmG (8) and DATMe-ImmG (9) displayed the lowest inhibition constants of 2.1 and 3.4 pM, respectively, vs PNP. It was postulated that the flexible natures of 8 and 9 enabled them to adopt conformations resembling those of 1 and 2 within the active site of PNP and that the positioning of two hydroxyl groups was critical for picomolar activity. SerMe-ImmH (10, K(d) = 5.2 pM) was shown to be orally available in mice with a long biological residence time on blood PNP.

Topics: Adenine; Adenosine; Catalytic Domain; Drug Design; Humans; Molecular Conformation; Pliability; Protein Binding; Purine-Nucleoside Phosphorylase; Pyrrolidines; Structure-Activity Relationship

2009