1207604-45-2Relevant academic research and scientific papers
A Comprehensive Landscape for Fibril Association Behaviors Encoded Synergistically by Saccharides and Peptides
Liu, Rongying,Zhang, Ran,Li, Long,Kochovski, Zdravko,Yao, Lintong,Nieh, Mu-Ping,Lu, Yan,Shi, Tongfei,Chen, Guosong
supporting information, p. 6622 - 6633 (2021/05/29)
Nature provides us a panorama of fibrils with tremendous structural polymorphism from molecular building blocks to hierarchical association behaviors. Despite recent achievements in creating artificial systems with individual building blocks through self-
Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasome's chymotrypsin-like sites
Geurink, Paul P.,Liu, Nora,Spaans, Michiel P.,Downey, Sondra L.,Van Den Nieuwendijk, Adrianus M. C. H.,Van Der Marel, Gijsbert A.,Kisselev, Alexei F.,Florea, Bogdan I.,Overkleeft, Herman S.
supporting information; experimental part, p. 2319 - 2323 (2010/08/06)
Proteasomal processing is conducted by three individual catalytic subunits, namely β11, β2, and β5. Subunit-specific inhibitors are useful tools in dissecting the role of these individual subunits and are leads toward the development of antitumor agents. We here report that the presence of fluorinated phenylalanine derivatives in peptide based proteasome inhibitors has a profound effect on inhibitor potency and selectivity. Specifically, compound 4a emerges as one of the most β5 specific inhibitors known to date.
