244782-33-0Relevant academic research and scientific papers
Design, synthesis and docking studies of novel dipeptidyl boronic acid proteasome inhibitors constructed from αα- and αβ-amino acids
Shi, Jingmiao,Lei, Meng,Wu, Wenkui,Feng, Huayun,Wang, Jia,Chen, Shanshan,Zhu, Yongqiang,Hu, Shihe,Liu, Zhaogang,Jiang, Cheng
supporting information, p. 1958 - 1962 (2016/04/05)
A series of novel dipeptidyl boronic acid proteasome inhibitors constructed from αα- and αβ-amino acids were designed and synthesized. Their structures were elucidated by 1H NMR, 13C NMR, LC-MS and HRMS. These compounds were evaluated for their β5 subunit inhibitory activities of human proteasome. The results showed that dipeptidyl boronic acid inhibitors composed of αα-amino acids were as active as bortezomib. Interestingly, the activities of those derived from αβ-amino acids lost completely. Of all the inhibitors, compound 22 (IC50 = 4.82 nM) was the most potent for the inhibition of proteasome activity. Compound 22 was also the most active against three MM cell lines with IC50 values less than 5 nM in inhibiting cell growth assays. Molecular docking studies displayed that 22 fitted very well in the β5 subunit active pocket of proteasome.
Observations on the deprotection of pinanediol and pinacol boronate esters via fluorinated intermediates
Inglis, Steven R.,Woon, Esther C. Y.,Thompson, Amber L.,Schofield, Christopher J.
supporting information; experimental part, p. 468 - 471 (2010/03/25)
(Chemical Equation Presented) Methods for the deprotection of pinanediol and pinacol esters of various boronic acids via fluoroborane intermediates were evaluated. Treatment of the boronate esters with potassium hydrogen difluoride normally gives trifluor
Stability of boronic esters to hydrolysis: A comparative study
Bernardini, Raffaella,Oliva, Ambrogio,Paganelli, Alessandro,Menta, Ernesto,Grugni, Mario,De Munari, Sergio,Goldoni, Luca
supporting information; experimental part, p. 750 - 751 (2011/04/21)
Boronic esters are key intermediates in the synthesis of biologically active compounds such as thrombin and proteasome inhibitors. However, they have low hydrolytic stability both during synthetic reactions and in biological media. We report the preparati
P1 Phenethyl peptide boronic acid inhibitors of HCV NS3 protease
Priestley,De Lucca, Indawati,Ghavimi, Bahman,Erickson-Viitanen, Susan,Decicco, Carl P.
, p. 3199 - 3202 (2007/10/03)
A series of peptide boronic acids containing extended, hydrophobic P1 residues was prepared to probe the shallow, hydrophobic S1 region of HCV NS3 protease. The p-trifluoromethylphenethyl P1 substituent was identified as optimal with respect to inhibitor potency for NS3 and selectivity against elastase and chymotrypsin.
