1207604-38-3Relevant academic research and scientific papers
Self-assembly of a tripeptide into a functional coating that resists fouling
Maity, Sibaprasad,Nir, Sivan,Zada, Tal,Reches, Meital
, p. 11154 - 11157 (2014/11/08)
This communication describes the self-assembly of a tripeptide into a functional coating that resists biofouling. Using this peptide-based coating we were able to prevent protein adsorption and interrupt biofilm formation. This coating can be applied on numerous substrates and therefore can serve in applications related to health care, marine and water treatment.
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.
