366803-66-9Relevant academic research and scientific papers
Structurally novel highly potent proteasome inhibitors created by the structure-based hybridization of nonpeptidic belactosin derivatives and peptide boronates
Kawamura, Shuhei,Unno, Yuka,Asai, Akira,Arisawa, Mitsuhiro,Shuto, Satoshi
supporting information, p. 2726 - 2735 (2014/04/17)
We previously developed highly potent proteasome inhibitor 1 (IC 50 = 5.7 nM) and its nonpeptide derivative 2 (IC50 = 29 nM) by systematic structure-activity relationship studies of the peptidic natural product belactosin A and subsequent rational topology-based scaffold hopping, respectively. Their cell growth inhibitory activities, however, were only moderate (IC50 = 1.8 μM (1) and >10 μM (2)). We therefore planned to replace the unstable β-lactone warhead with a more stable boronic acid warhead. Importantly, belactosin derivatives bind mainly to the proteasome binding site, which is different from that occupied by known peptide boronate proteasome inhibitors such as bortezomib, suggesting that their hybridization might lead to the development of novel potent inhibitors. Here we describe design, synthesis, and biological activities of the newly developed potent hybrid proteasome inhibitors. Interestingly, these hybrids, unlike bortezomib, were highly selective for proteasomes and have long residence times despite having the same boronic acid warhead.
Acetonyltriphenylphosphonium bromide in organic synthesis: A useful catalyst in the cyclotrimerization of aldehydes
Hon, Yung-Son,Lee, Chia-Fu
, p. 6181 - 6188 (2007/10/03)
Acetonyltriphenylphosphonium bromide (ATPB) is a useful catalyst for the cyclotrimerization of the aliphatic aldehydes under solvent-free condition. The aldehydes tethered with a variety of functionality such as olefin, ether, ester, bromide, azide and diester could also be cyclotrimerized under the catalysis of ATPB.
