102922-72-5Relevant articles and documents
Selective Targeting of AF9 YEATS Domain by Cyclopeptide Inhibitors with Preorganized Conformation
Jiang, Yixiang,Chen, Guochao,Li, Xiao-Meng,Liu, Sha,Tian, Gaofei,Li, Yuanyuan,Li, Xin,Li, Haitao,Li, Xiang David
, p. 21450 - 21459 (2020)
YEATS domains are newly identified epigenetic "readers"of histone lysine acetylation (Kac) and crotonylation (Kcr). The malfunction of YEATS-Kac/Kcr interactions has been found to be involved in the pathogenesis of human diseases, such as cancer. These di
Development of a Highly Selective Plasmodium falciparum Proteasome Inhibitor with Anti-malaria Activity in Humanized Mice
Zhan, Wenhu,Zhang, Hao,Ginn, John,Leung, Annie,Liu, Yi J.,Michino, Mayako,Toita, Akinori,Okamoto, Rei,Wong, Tzu-Tshin,Imaeda, Toshihiro,Hara, Ryoma,Yukawa, Takafumi,Chelebieva, Sevil,Tumwebaze, Patrick K.,Lafuente-Monasterio, Maria Jose,Martinez-Martinez, Maria Santos,Vendome, Jeremie,Beuming, Thijs,Sato, Kenjiro,Aso, Kazuyoshi,Rosenthal, Philip J.,Cooper, Roland A.,Meinke, Peter T.,Nathan, Carl F.,Kirkman, Laura A.,Lin, Gang
supporting information, p. 9279 - 9283 (2021/03/18)
Plasmodium falciparum proteasome (Pf20S) inhibitors are active against Plasmodium at multiple stages—erythrocytic, gametocyte, liver, and gamete activation stages—indicating that selective Pf20S inhibitors possess the potential to be therapeutic, prophyla
Orthogonally protected artificial amino acid as tripod ligand for automated peptide synthesis and labeling with [99mTc(OH2) 3(CO)3]+
Shen, Yunjun,Schottelius, Margret,Zelenka, Karel,De Simone, Mariarosaria,Pohle, Karolin,Kessler, Horst,Wester, Hans-Jürgen,Schmutz, Paul,Alberto, Roger
, p. 26 - 35 (2013/03/28)
1,2-Diamino-propionic acid (Dap) is a very strong chelator for the [ 99mTc(CO)3]+ core, yielding small and hydrophilic complexes. We prepared the lysine based Dap derivative l-Lys(Dap) in which the ε-NH2 group was replaced by the tripod through conjugation to its α-carbon. The synthetic strategy produced an orthogonally protected bifunctional chelator (BFC). The -NH2 group of the α-amino acid portion is Fmoc- and the -NH2 of Dap are Boc-protected. Fmoc-l-Lys(Dap(Boc)) was either conjugated to the N- and C-terminus of bombesin BBN(7-14) or integrated into the sequence using solid-phase peptide synthesis (SPPS). We also replaced the native lysine in a cyclic RGD peptide with l-Lys(Dap). For all peptides, quantitative labeling with the [99mTc(CO)3]+ core at a 10 μM concentration in PBS buffer (pH = 7.4) was achieved. For comparison, the rhenium homologues were prepared from [Re(OH2)3(CO) 3]+ and Lys(Dap)-BBN(7-14) or cyclo-(RGDyK(Dap)), respectively. Determination of integrin receptor binding showed low to medium nanomolar affinities for various receptor subtypes. The IC50 of cyclo-(RGDyK(Dap[Re(CO)3])) for αvβ3 is 7.1 nM as compared to 3.1 nM for nonligated RGD derivative. Biodistribution studies in M21 melanoma bearing nude mice showed reasonable α vβ3-integrin specific tumor uptake. Altogether, orthogonally protected l-Lys(Dap) represents a highly versatile building block for integration in any peptide sequence. Lys(Dap)-precursors allow high-yield 99mTc-labeling with [99mTc(OH2) 3(CO)3]+, forming small and hydrophilic complexes, which in turn leads to peptide radiopharmaceuticals with excellent in vivo characteristics.
